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	<id>https://www.cazypedia.org/api.php?action=feedcontributions&amp;feedformat=atom&amp;user=Plinio+Vieira</id>
	<title>CAZypedia - User contributions [en-ca]</title>
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	<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php/Special:Contributions/Plinio_Vieira"/>
	<updated>2026-05-04T22:01:12Z</updated>
	<subtitle>User contributions</subtitle>
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	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17126</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17126"/>
		<updated>2023-03-24T14:33:02Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Psvieira.jpg|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the engineering and evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH1]] ''Em''Bgl &amp;lt;cite&amp;gt;Sousa2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH8]] ''Xac''Cel8A &amp;lt;cite&amp;gt;Melo2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ 6UAS] [https://www.rcsb.org/structure/6UFL 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Sousa2020 de Sousa, A.S., de Melo, R.R., Miyamoto, R.Y., Morais, M.A.B., Andrade, L.P., Milan, N., de Avila, M.C., de Souza, C.M., Adão, R.C., Scarpassa, J.A., Vieira, P.S., dos Santos, L.V., Ramos, C.H.I., Murakami, M.T. and Zanphorlin, L.M. (2020). ''A rationally identified marine GH1 β-glucosidase has distinguishing functional features for simultaneous saccharification and fermentation''. ''Biofuels, Bioprod. Bioref.'' 2020;'''14'''(6):1163-1179. [https://dx.doi.org/10.1002/bbb.2136 DOI: 10.1002/bbb.2136]&lt;br /&gt;
&lt;br /&gt;
#Melo2021 pmid=33164774&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17125</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17125"/>
		<updated>2023-03-24T14:32:39Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Psvieira.jpg|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the engineering and evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH1]] ''Em''Bgl &amp;lt;cite&amp;gt;Sousa2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH8]] ''Xac''Cel8A &amp;lt;cite&amp;gt;Melo2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ 6UAS] [https://www.rcsb.org/structure/6UFL 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Sousa2020 de Sousa, A.S., de Melo, R.R., Miyamoto, R.Y., Morais, M.A.B., Andrade, L.P., Milan, N., de Avila, M.C., de Souza, C.M., Adão, R.C., Scarpassa, J.A., Vieira, P.S., dos Santos, L.V., Ramos, C.H.I., Murakami, M.T. and Zanphorlin, L.M. (2020). ''A rationally identified marine GH1 β-glucosidase has distinguishing functional features for simultaneous saccharification and fermentation''. ''Biofuels, Bioprod. Bioref.''. 2020;'''14'''(6):1163-1179. [https://dx.doi.org/10.1002/bbb.2136 DOI: 10.1002/bbb.2136]&lt;br /&gt;
&lt;br /&gt;
#Melo2021 pmid=33164774&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17124</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17124"/>
		<updated>2023-03-24T14:29:45Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Psvieira.jpg|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the engineering and evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH1]] ''Em''Bgl &amp;lt;cite&amp;gt;Sousa2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH8]] ''Xac''Cel8A &amp;lt;cite&amp;gt;Melo2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ 6UAS] [https://www.rcsb.org/structure/6UFL 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Sousa2020 de Sousa, A.S., de Melo, R.R., Miyamoto, R.Y., Morais, M.A.B., Andrade, L.P., Milan, N., de Avila, M.C., de Souza, C.M., Adão, R.C., Scarpassa, J.A., Vieira, P.S., dos Santos, L.V., Ramos, C.H.I., Murakami, M.T. and Zanphorlin, L.M. (2020). ''A rationally identified marine GH1 β-glucosidase has distinguishing functional features for simultaneous saccharification and fermentation''. ''Biofuels, Bioprod. Bioref.''. 2020;'''14''':1163-1179. [https://dx.doi.org/10.1002/bbb.2136 DOI: 10.1002/bbb.2136]&lt;br /&gt;
&lt;br /&gt;
#Melo2021 pmid=33164774&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17123</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17123"/>
		<updated>2023-03-24T14:29:21Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Psvieira.jpg|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the engineering and evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH1]] ''Em''Bgl &amp;lt;cite&amp;gt;Sousa2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH8]] ''Xac''Cel8A &amp;lt;cite&amp;gt;Melo2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ 6UAS] [https://www.rcsb.org/structure/6UFL 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Sousa2020 de Sousa, A.S., de Melo, R.R., Miyamoto, R.Y., Morais, M.A.B., Andrade, L.P., Milan, N., de Avila, M.C., de Souza, C.M., Adão, R.C., Scarpassa, J.A., Vieira, P.S., dos Santos, L.V., Ramos, C.H.I., Murakami, M.T. and Zanphorlin, L.M. (2020). ''A rationally identified marine GH1 β-glucosidase has distinguishing functional features for simultaneous saccharification and fermentation''. ''Biofuels, Bioprod. Bioref.''. 2020;'''14''':1163-1179. [https://dx.doi.org/10.1002/bbb.2136 DOI: 10.1002/bbb.2136&lt;br /&gt;
&lt;br /&gt;
#Melo2021 pmid=33164774&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17122</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17122"/>
		<updated>2023-03-24T14:28:09Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Psvieira.jpg|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the engineering and evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH1]] ''Em''Bgl &amp;lt;cite&amp;gt;Sousa2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH8]] ''Xac''Cel8A &amp;lt;cite&amp;gt;Melo2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ 6UAS] [https://www.rcsb.org/structure/6UFL 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Sousa2020 de Sousa, A.S., de Melo, R.R., Miyamoto, R.Y., Morais, M.A.B., Andrade, L.P., Milan, N., de Avila, M.C., de Souza, C.M., Adão, R.C., Scarpassa, J.A., Vieira, P.S., dos Santos, L.V., Ramos, C.H.I., Murakami, M.T. and Zanphorlin, L.M. (2020). ''A rationally identified marine GH1 β-glucosidase has distinguishing functional features for simultaneous saccharification and fermentation''. ''Biofuels, Bioprod. Bioref.''. 2020;'''14''':1163-1179. https://doi-org/10.1002/bbb.2136&lt;br /&gt;
&lt;br /&gt;
#Melo2021 pmid=33164774&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17121</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17121"/>
		<updated>2023-03-24T14:27:25Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Psvieira.jpg|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the engineering and evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH1]] ''Em''Bgl &amp;lt;cite&amp;gt;Sousa2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH8]] ''Xac''Cel8A &amp;lt;cite&amp;gt;Melo2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ 6UAS] [https://www.rcsb.org/structure/6UFL 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Sousa2020 de Sousa, A.S., de Melo, R.R., Miyamoto, R.Y., Morais, M.A.B., Andrade, L.P., Milan, N., de Avila, M.C., de Souza, C.M., Adão, R.C., Scarpassa, J.A., Vieira, P.S., dos Santos, L.V., Ramos, C.H.I., Murakami, M.T. and Zanphorlin, L.M. (2020). ''A rationally identified marine GH1 β-glucosidase has distinguishing functional features for simultaneous saccharification and fermentation''. ''Biofuels, Bioprod. Bioref.''. 2020;'''14''':1163-1179. [[https://doi-org/10.1002/bbb.2136]]&lt;br /&gt;
&lt;br /&gt;
#Melo2021 pmid=33164774&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17120</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17120"/>
		<updated>2023-03-23T17:24:15Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Psvieira.jpg|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the engineering and evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ 6UAS] [https://www.rcsb.org/structure/6UFL 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17119</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17119"/>
		<updated>2023-03-23T11:42:53Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic residues ==&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through Glycine backbone, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as is expected for other related carbohydrate esterase (CE) families [[CE2]], [[CE3]], [[CE6]], [[CE12]] and [[CE17]], that harbour the SGNH-hydrolase fold.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG. ''Xac''XaeA showed lower activity towards metanoate compared to the prefered substrate acetate, but catalysis was not observed for longer chains &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17118</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17118"/>
		<updated>2023-03-23T11:32:11Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic residues ==&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as is expected for other related carbohydrate esterase (CE) families [[CE2]], [[CE3]], [[CE6]], [[CE12]] and [[CE17]] that harbour the SGNH-hydrolase fold.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG. ''Xac''XaeA showed lower activity towards metanoate compared to the prefered substrate acetate, but catalysis was not observed for longer chains &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17117</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17117"/>
		<updated>2023-03-23T11:22:30Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic residues ==&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families [[CE2]], [[CE3]], [[CE6]], [[CE12]] and [[CE17]].&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG. ''Xac''XaeA showed lower activity towards metanoate compared to the prefered substrate acetate, but catalysis was not observed for longer chains &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17116</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17116"/>
		<updated>2023-03-23T11:17:06Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic residues ==&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present and well conserved in ''Xanthomonas'' proteins, denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17115</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17115"/>
		<updated>2023-03-23T11:15:29Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic residues ==&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a), showed in cartoon and surface representations. Catalytic residues are circled, in brown sticks. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps, represented in (c) as pink surface. Domains in (b) and (c) are annotated according to (a). Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present and participating in the oxyanion hole through residues' backbone, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17114</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17114"/>
		<updated>2023-03-22T19:41:56Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic residues ==&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|'''Figure 1:''' The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a). Catalytic residues are circled. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps. Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17113</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17113"/>
		<updated>2023-03-22T19:41:06Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic residues ==&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|Figure 1: The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a). Catalytic residues are circled. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps. Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17112</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17112"/>
		<updated>2023-03-22T19:38:56Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|Figure 1: The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a). Catalytic residues are circled. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps. Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]&lt;br /&gt;
== Catalytic residues ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17111</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17111"/>
		<updated>2023-03-22T19:38:25Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic residues ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17110</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17110"/>
		<updated>2023-03-22T19:33:22Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|Figure 1: The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a). Catalytic residues are circled. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps. Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]&lt;br /&gt;
== Catalytic residues ==''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17109</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17109"/>
		<updated>2023-03-22T19:32:45Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|Figure 1: The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a). Catalytic residues are circled. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps. Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]== Catalytic residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17108</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17108"/>
		<updated>2023-03-22T19:32:11Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|Figure 1: The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a). Catalytic residues are circled. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps. Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].]]== Catalytic Residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17107</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17107"/>
		<updated>2023-03-22T19:31:21Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved electropositive oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|Figure 1: The tridimensional structure and architecture of ''Xac''XaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) Structural topology, delimited by domains and (c) crystal structure, color-coded according to (a). Catalytic residues are circled. X448 domain is absent in the tridimensional model due to proteolysis removal in the crystallization steps. Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License]]].&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17106</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17106"/>
		<updated>2023-03-22T19:26:49Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|Figure 1: The tridimensional structure and architecture of XacXaeA, the founding member of CE20 family. [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] (a) Domain organization showing the position of catalytic residues (red triangles). (b) structural topology and (c) crystal structure color-coded according to (a). Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License]]].&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17105</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17105"/>
		<updated>2023-03-22T19:04:17Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|Figure 1: Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License]]].&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17104</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17104"/>
		<updated>2023-03-22T19:00:04Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H''') (Infered catalytic residues in bold). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|500px|Figure 1: Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License]]].&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17103</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17103"/>
		<updated>2023-03-22T18:59:12Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H'''). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|400px|Figure 1: Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License]]].&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17102</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17102"/>
		<updated>2023-03-22T18:58:51Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H'''). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|300px|Figure 1: Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License]]].&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17101</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17101"/>
		<updated>2023-03-22T18:49:35Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H'''). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|300px|Figure 1: Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License]]].&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17100</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17100"/>
		<updated>2023-03-22T18:49:02Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQ'''S'''NME) and Block V ('''D'''I'''H'''). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
&lt;br /&gt;
[[Image:Ce20_cazypedia.png|thumb|300px|Figure 1: Adapted from &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; originally published under [http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International License].&lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17099</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17099"/>
		<updated>2023-03-22T18:30:08Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions in ''Xanthomonas'', denoted as Block I (GQSNME) and Block V (DxH). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop.&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=File:Ce20_cazypedia.png&amp;diff=17098</id>
		<title>File:Ce20 cazypedia.png</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=File:Ce20_cazypedia.png&amp;diff=17098"/>
		<updated>2023-03-22T18:28:29Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;Architecture and tridimensional structure of CE20 member XacXaeA&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17097</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17097"/>
		<updated>2023-03-22T18:01:31Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions named Block I (GQSNME) and Block V (DxH). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, as noted for other related carbohydrate esterase (CE) families.&amp;lt;br&amp;gt;&amp;lt;br&amp;gt;&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
The founding member of this family seems to have the canonical catalytic triad Ser-Asp-His found in esterases from other families &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, but this inference still requires experimental validation.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop . &lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17096</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17096"/>
		<updated>2023-03-22T17:56:15Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions named Block I (GQSNME), a modified version of the classical nucleophilic elbow from proteases; and Block V (DxH). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent, as noted for other related carbohydrate esterase (CE) families.&amp;lt;br&amp;gt;&amp;lt;br&amp;gt;&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
The founding member of this family seems to have the canonical catalytic triad Ser-Asp-His found in esterases from other families &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, but this inference still requires experimental validation.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop . &lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17095</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17095"/>
		<updated>2023-03-22T17:55:58Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions named Block I (GQSNME), a modified version of the classical nucleophilic elbow from proteases; and Block V (DxH). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent, as noted for other related carbohydrate esterase (CE) families.&amp;lt;br&amp;gt;&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
The founding member of this family seems to have the canonical catalytic triad Ser-Asp-His found in esterases from other families &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, but this inference still requires experimental validation.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop . &lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17094</id>
		<title>Carbohydrate Esterase Family 20</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_20&amp;diff=17094"/>
		<updated>2023-03-22T17:55:27Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;&amp;lt;!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --&amp;gt;&lt;br /&gt;
{{UnderConstruction}}&lt;br /&gt;
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]&lt;br /&gt;
* [[Responsible Curator]]:  [[User:Mario Murakami|Mario Murakami]]&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- The data in the table below should be updated by the Author/Curator according to current information on the family --&amp;gt;&lt;br /&gt;
&amp;lt;div style=&amp;quot;float:right&amp;quot;&amp;gt;&lt;br /&gt;
{| {{Prettytable}} &lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''Carbohydrate Esterase Family CE20'''&lt;br /&gt;
|-&lt;br /&gt;
|'''Fold'''    &lt;br /&gt;
|β-sandwich/(α-β-α) sandwich/β-sandwich&lt;br /&gt;
|-&lt;br /&gt;
|'''Mechanism'''&lt;br /&gt;
|serine hydrolase&lt;br /&gt;
|-&lt;br /&gt;
|'''Active site residues'''&lt;br /&gt;
|known&lt;br /&gt;
|-&lt;br /&gt;
|{{Hl2}} colspan=&amp;quot;2&amp;quot; align=&amp;quot;center&amp;quot; |'''CAZy DB link'''&lt;br /&gt;
|-&lt;br /&gt;
| colspan=&amp;quot;2&amp;quot; |{{CAZyDBlink}}CE20.html&lt;br /&gt;
|}&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&amp;lt;!-- This is the end of the table --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
== Substrate specificities ==&lt;br /&gt;
Carbohydrate esterase family 20 (CE20) currently comprises  xyloglucan acetylesterases (E.C. [https://www.enzyme-database.org/query.php?ec=3.1.1.6 3.2.1.6]) &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt; and acetylesterases putatively related to arabinoxylan deacetylation &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt; .&lt;br /&gt;
&lt;br /&gt;
== Kinetics and Mechanism ==&lt;br /&gt;
''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, harbors the canonical catalytic triad Ser-Asp-His and the conserved oxyanion hole. Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE3]] and [[CE6]]. However, this assumption still requires experimental validation. The catalytic-relevant residues are present in consensus regions named Block I (GQSNME), a modified version of the classical nucleophilic elbow from proteases; and Block V (DxH). Oxyanion hole residues are present in Blocks I (GQSNME) and III (YQGET). Although consensus Block II is present, Block IV is absent, as noted for other related carbohydrate esterase (CE) families.&lt;br /&gt;
''Xac''XaeA is specific to ''O''-acetylation since it is not capable of cleaving ''N''-acetylated carbohydrates. It shows activity on a broad range of ''O''-acetylated mono- and disaccharides and did not show a positional preference for acetylated oxygens. ''Xac''XaeA was active towards cell wall extracted xyloglucan oligosaccharides, deacetylating distinct types of structures such as XXLG/XLXG, XXFG, and XLFG &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate &amp;lt;cite&amp;gt;Liu2022&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
== Catalytic Residues ==&lt;br /&gt;
The founding member of this family seems to have the canonical catalytic triad Ser-Asp-His found in esterases from other families &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, but this inference still requires experimental validation.&lt;br /&gt;
&lt;br /&gt;
== Three-dimensional structures ==&lt;br /&gt;
The CE20 structure is composed of a central catalytic core, which displays the SGNH hydrolase fold, flanked by two antiparallel seven-stranded β-sandwiches intimately linked to the central core, forming a monolithic structure &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;. Such structural architecture diverges from CE families described in the CAZy database so far. In ''Xac''XaeA, the founding member of family CE20 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;, the catalytic core is composed of two halves (residues 104-216 and 397-541) due to the insertion of a domain (residues 217-396, named X448 in the CAZy database &amp;lt;cite&amp;gt;Cantarel2009 DaviesSinnott2008&amp;lt;/cite&amp;gt;) in the α5-η3 loop . &lt;br /&gt;
&lt;br /&gt;
== Family Firsts ==&lt;br /&gt;
;First stereochemistry determination: Content is to be added here.&lt;br /&gt;
;First catalytic nucleophile identification: Content is to be added here.&lt;br /&gt;
;First general acid/base residue identification: Content is to be added here.&lt;br /&gt;
&lt;br /&gt;
;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
&lt;br /&gt;
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;.&lt;br /&gt;
== References ==&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
#Cantarel2009 pmid=18838391&lt;br /&gt;
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Liu2022 pmid=36403068&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
[[Category:Carbohydrate Esterase Families|CE020]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17089</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17089"/>
		<updated>2023-03-22T17:21:19Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Psvieira.jpg|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the engineering and evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=File:Psvieira.jpg&amp;diff=17088</id>
		<title>File:Psvieira.jpg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=File:Psvieira.jpg&amp;diff=17088"/>
		<updated>2023-03-22T17:17:54Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;-&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=File:Pvieira.jpg&amp;diff=17086</id>
		<title>File:Pvieira.jpg</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=File:Pvieira.jpg&amp;diff=17086"/>
		<updated>2023-03-22T17:15:49Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;-&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17085</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17085"/>
		<updated>2023-03-22T17:13:54Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the engineering and evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17083</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17083"/>
		<updated>2023-03-22T15:42:48Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the engineering and evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17082</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17082"/>
		<updated>2023-03-22T15:40:55Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function relationship from CAZymes. He has contributed for the tridimensional structure determination and biochemical characterization of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17081</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17081"/>
		<updated>2023-03-22T15:37:44Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] [https://www.rcsb.org/structure/6BYI PDB ID 6BYI][https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17080</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17080"/>
		<updated>2023-03-22T15:35:48Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17079</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17079"/>
		<updated>2023-03-22T15:34:48Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' [https://www.rcsb.org/structure/7KMM ''Xac''XaeA] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17078</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17078"/>
		<updated>2023-03-22T15:34:17Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17077</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17077"/>
		<updated>2023-03-22T15:34:04Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' Xac''XaeA [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17076</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17076"/>
		<updated>2023-03-22T15:33:42Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' 'Xac''XaeA [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17052</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17052"/>
		<updated>2023-01-24T20:23:00Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also worked on a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xanthomonas citri'' pv. ''citri'' xyloglucan acetylesterase (''Xac''XaeA) [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase (''Xac''Man2A) [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase, in complex with mannose (''Xac''Man2A) [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase mutant E477A (''Xac''Man2A) [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase mutant E575A (''Xac''Man2A) [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;alpha;-xylosidase (''Xac''Xyl31) [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;alpha;-xylosidase, in complex with xylose (''Xac''Xyl31) [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-galactosidase (''Xac''GalD) [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-galactosidase, in complex with galactose (''Xac''GalD) [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xanthomonas campestris'' pv. ''campestris'' endo-xyloglucanase, in complex with XG oligosaccharide (''Xcc''Xeg74) [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xanthomonas citri'' pv. ''citri'' &amp;amp;alpha;-L-1,2-fucosidase (''Xac''Afc95) [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E102A mutant, in complex with laminaritriose and laminaribiose (AmGH128_I) [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E102A mutant, in complex with laminaripentaose (AmGH128_I) [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199Q mutant (AmGH128_I) [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199A mutant, in complex with laminaripentaose (AmGH128_I) [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199A mutant, in complex with laminarihexaose (AmGH128_I) [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Sorangium cellulosum'' endo-&amp;amp;beta;-1,3-glucanase (ScGH128_II) [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Lentinula edodes'' endo-&amp;amp;beta;-1,3-glucanase (LeGH128_IV) [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase (AnGH128_VI) [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase, in complex with laminaritriose (AnGH128_VI) [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase, with laminaribiose at the surface-binding site (AnGH128_VI) [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Cryptococcus neoformans'' oligosaccharide-binding protein (CnGH128_VII) [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17051</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17051"/>
		<updated>2023-01-24T20:21:55Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Salmazo Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also developed a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xanthomonas citri'' pv. ''citri'' xyloglucan acetylesterase (''Xac''XaeA) [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase (''Xac''Man2A) [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase, in complex with mannose (''Xac''Man2A) [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase mutant E477A (''Xac''Man2A) [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase mutant E575A (''Xac''Man2A) [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;alpha;-xylosidase (''Xac''Xyl31) [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;alpha;-xylosidase, in complex with xylose (''Xac''Xyl31) [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-galactosidase (''Xac''GalD) [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-galactosidase, in complex with galactose (''Xac''GalD) [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xanthomonas campestris'' pv. ''campestris'' endo-xyloglucanase, in complex with XG oligosaccharide (''Xcc''Xeg74) [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xanthomonas citri'' pv. ''citri'' &amp;amp;alpha;-L-1,2-fucosidase (''Xac''Afc95) [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E102A mutant, in complex with laminaritriose and laminaribiose (AmGH128_I) [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E102A mutant, in complex with laminaripentaose (AmGH128_I) [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199Q mutant (AmGH128_I) [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199A mutant, in complex with laminaripentaose (AmGH128_I) [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199A mutant, in complex with laminarihexaose (AmGH128_I) [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Sorangium cellulosum'' endo-&amp;amp;beta;-1,3-glucanase (ScGH128_II) [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Lentinula edodes'' endo-&amp;amp;beta;-1,3-glucanase (LeGH128_IV) [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase (AnGH128_VI) [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase, in complex with laminaritriose (AnGH128_VI) [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase, with laminaribiose at the surface-binding site (AnGH128_VI) [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Cryptococcus neoformans'' oligosaccharide-binding protein (CnGH128_VII) [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17050</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17050"/>
		<updated>2023-01-24T20:16:27Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also developed a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xanthomonas citri'' pv. ''citri'' xyloglucan acetylesterase (''Xac''XaeA) [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase (''Xac''Man2A) [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase, in complex with mannose (''Xac''Man2A) [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase mutant E477A (''Xac''Man2A) [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase mutant E575A (''Xac''Man2A) [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;alpha;-xylosidase (''Xac''Xyl31) [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;alpha;-xylosidase, in complex with xylose (''Xac''Xyl31) [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-galactosidase (''Xac''GalD) [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-galactosidase, in complex with galactose (''Xac''GalD) [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xanthomonas campestris'' pv. ''campestris'' endo-xyloglucanase, in complex with XG oligosaccharide (''Xcc''Xeg74) [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xanthomonas citri'' pv. ''citri'' &amp;amp;alpha;-L-1,2-fucosidase (''Xac''Afc95) [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E102A mutant, in complex with laminaritriose and laminaribiose (AmGH128_I) [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E102A mutant, in complex with laminaripentaose (AmGH128_I) [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199Q mutant (AmGH128_I) [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199A mutant, in complex with laminaripentaose (AmGH128_I) [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199A mutant, in complex with laminarihexaose (AmGH128_I) [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Sorangium cellulosum'' endo-&amp;amp;beta;-1,3-glucanase (ScGH128_II) [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Lentinula edodes'' endo-&amp;amp;beta;-1,3-glucanase (LeGH128_IV) [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase (AnGH128_VI) [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase, in complex with laminaritriose (AnGH128_VI) [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase, with laminaribiose at the surface-binding site (AnGH128_VI) [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Cryptococcus neoformans'' oligosaccharide-binding protein (CnGH128_VII) [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17049</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17049"/>
		<updated>2023-01-24T20:09:57Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
&lt;br /&gt;
Plinio Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also developed a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
&lt;br /&gt;
*[[CE20]] '''Family first''' ''Xanthomonas citri'' pv. ''citri'' xyloglucan acetylesterase [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase, in complex with mannose [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase mutant E477A [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase mutant E575A [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;alpha;-xylosidase [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;alpha;-xylosidase, in complex with xylose [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-galactosidase [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-galactosidase, in complex with galactose [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xanthomonas campestris'' pv. ''campestris'' endo-xyloglucanase, in complex with XG oligosaccharide [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xanthomonas citri'' pv. ''citri'' &amp;amp;alpha;-L-1,2-fucosidase [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E102A mutant, in complex with laminaritriose and laminaribiose [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E102A mutant, in complex with laminaripentaose [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199Q mutant [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199A mutant, in complex with laminaripentaose [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199A mutant, in complex with laminarihexaose [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Sorangium cellulosum'' endo-&amp;amp;beta;-1,3-glucanase [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Lentinula edodes'' endo-&amp;amp;beta;-1,3-glucanase [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase, in complex with laminaritriose [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase, with laminaribiose at the surface-binding site [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH128]] ''Cryptococcus neoformans'' oligosaccharide-binding protein [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;cite&amp;gt;Santos2020&amp;lt;/cite&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&lt;br /&gt;
&amp;lt;/div&amp;gt;&amp;lt;div&amp;gt;&lt;br /&gt;
&amp;lt;/div&amp;gt;&amp;lt;div&amp;gt;&lt;br /&gt;
&amp;lt;/div&amp;gt;&lt;br /&gt;
&lt;br /&gt;
----&lt;br /&gt;
&lt;br /&gt;
&amp;lt;biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
#Vieira2021 pmid=34193873&lt;br /&gt;
&lt;br /&gt;
#Santos2020 pmid=32451508&lt;br /&gt;
&lt;br /&gt;
#Domingues2018 pmid=29997257&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
&lt;br /&gt;
&amp;lt;!-- Do not remove this Category tag --&amp;gt;&lt;br /&gt;
&lt;br /&gt;
[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
	</entry>
	<entry>
		<id>https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17048</id>
		<title>User:Plinio Vieira</title>
		<link rel="alternate" type="text/html" href="https://www.cazypedia.org/index.php?title=User:Plinio_Vieira&amp;diff=17048"/>
		<updated>2023-01-24T20:08:40Z</updated>

		<summary type="html">&lt;p&gt;Plinio Vieira: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;[[Image:Blank user-200px.png|200px|right]]&lt;br /&gt;
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Plinio Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also developed a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 &amp;amp;beta;-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:&lt;br /&gt;
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*[[CE20]] '''Family first''' ''Xanthomonas citri'' pv. ''citri'' xyloglucan acetylesterase [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] &amp;lt;cite&amp;gt;Vieira2021&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase, in complex with mannose [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] &amp;lt;cite&amp;gt;Domingues2018&amp;lt;/cite&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase mutant E477A [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] &amp;lt;ref&amp;gt;Domingues2018&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-mannanase mutant E575A [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] &amp;lt;ref&amp;gt;Domingues2018&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;alpha;-xylosidase [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] &amp;lt;ref&amp;gt;Vieira2021&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;alpha;-xylosidase, in complex with xylose [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] &amp;lt;ref&amp;gt;Vieira2021&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-galactosidase [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] &amp;lt;ref&amp;gt;Vieira2021&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&amp;amp;beta;-galactosidase, in complex with galactose [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] &amp;lt;ref&amp;gt;Vieira2021&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH74]] ''Xanthomonas campestris'' pv. ''campestris'' endo-xyloglucanase, in complex with XG oligosaccharide [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] &amp;lt;ref&amp;gt;Vieira2021&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH95]] ''Xanthomonas citri'' pv. ''citri'' &amp;amp;alpha;-L-1,2-fucosidase [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] &amp;lt;ref&amp;gt;Vieira2021&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E102A mutant, in complex with laminaritriose and laminaribiose [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E102A mutant, in complex with laminaripentaose [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199Q mutant [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199A mutant, in complex with laminaripentaose [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&amp;amp;beta;-1,3-glucanase E199A mutant, in complex with laminarihexaose [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Sorangium cellulosum'' endo-&amp;amp;beta;-1,3-glucanase [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Lentinula edodes'' endo-&amp;amp;beta;-1,3-glucanase [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase, in complex with laminaritriose [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Aureobasidium namibiae'' exo-&amp;amp;beta;-1,3-glucanase, with laminaribiose at the surface-binding site [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
*[[GH128]] ''Cryptococcus neoformans'' oligosaccharide-binding protein [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] &amp;lt;ref&amp;gt;Santos2020&amp;lt;/ref&amp;gt;&lt;br /&gt;
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&amp;lt;biblio&amp;gt;&lt;br /&gt;
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#Vieira2021 pmid=34193873&lt;br /&gt;
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#Santos2020 pmid=32451508&lt;br /&gt;
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#Domingues2018 pmid=29997257&lt;br /&gt;
&amp;lt;/biblio&amp;gt;&lt;br /&gt;
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[[Category:Contributors|Vieira,Plinio]]&lt;/div&gt;</summary>
		<author><name>Plinio Vieira</name></author>
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