CAZypedia - User contributions [en-ca]

Carbohydrate Esterase Family 20

2023-03-22T17:30:29Z

Priscila Giuseppe:

{{UnderConstruction}}
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE20'''
|-
|'''Fold'''
|β-sandwich/(α-β-α) sandwich/β-sandwich
|-
|'''Mechanism'''
|serine hydrolase
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE20.html
|}
</div>


== Substrate specificities ==
Carbohydrate esterase family 20 (CE20) currently comprises xyloglucan acetylesterases <cite>Vieira2021</cite> and acetylesterases putatively related to arabinoxylan deacetylation <cite>Liu2022</cite> .

== Kinetics and Mechanism ==
''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad (Asp-His-Ser). Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE1]]. However, this assumption still requires experimental validation. ''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 <cite>Vieira2021</cite>. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate <cite>Liu2022</cite>.
== Catalytic Residues ==
The founding member of this family seems to have the canonical catalytic triad (Asp-His-Ser) found in esterases from other families <cite>Vieira2021</cite>, but this inference still requires experimental validation.

== Three-dimensional structures ==
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 <cite>Vieira2021</cite>. Such structural architecture diverges from carbohydrate esterase (CE) families described in the CAZy database so far. In XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, 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 <cite>Cantarel2009 DaviesSinnott2008</cite>) in the α5-η3 loop .

== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
;First catalytic nucleophile identification: Content is to be added here.
;First general acid/base residue identification: Content is to be added here.

;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 <cite>Vieira2021</cite>.

;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 <cite>Vieira2021</cite>.
== References ==
<biblio>
#Cantarel2009 pmid=18838391
#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].

#Vieira2021 pmid=34193873

#Liu2022 pmid=36403068

</biblio>

[[Category:Carbohydrate Esterase Families|CE020]]

Carbohydrate Esterase Family 20

2023-03-22T17:29:36Z

Priscila Giuseppe:

{{UnderConstruction}}
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE20'''
|-
|'''Fold'''
|β-sandwich/(α-β-α) sandwich/β-sandwich
|-
|'''Mechanism'''
|serine hydrolase
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE20.html
|}
</div>


== Substrate specificities ==
Carbohydrate esterase family 20 (CE20) currently comprises xyloglucan acetylesterases <cite>Vieira2021</cite> and acetylesterases putatively related to arabinoxylan deacetylation <cite>Liu2022</cite> .

== Kinetics and Mechanism ==
''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad (Asp-His-Ser). Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE1]]. However, this assumption still requires experimental validation. ''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 <cite>Vieira2021</cite>. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate <cite>Liu2022</cite>.
== Catalytic Residues ==
The founding members of this family seem to have the canonical catalytic triad (Asp-His-Ser) found in esterases from other families <cite>Vieira2021</cite>, but this inference still requires experimental validation.

== Three-dimensional structures ==
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 <cite>Vieira2021</cite>. Such structural architecture diverges from carbohydrate esterase (CE) families described in the CAZy database so far. In XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, 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 <cite>Cantarel2009 DaviesSinnott2008</cite>) in the α5-η3 loop .

== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
;First catalytic nucleophile identification: Content is to be added here.
;First general acid/base residue identification: Content is to be added here.

;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 <cite>Vieira2021</cite>.

;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 <cite>Vieira2021</cite>.
== References ==
<biblio>
#Cantarel2009 pmid=18838391
#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].

#Vieira2021 pmid=34193873

#Liu2022 pmid=36403068

</biblio>

[[Category:Carbohydrate Esterase Families|CE020]]

Carbohydrate Esterase Family 20

2023-03-22T17:27:52Z

Priscila Giuseppe:

{{UnderConstruction}}
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE20'''
|-
|'''Fold'''
|β-sandwich/(α-β-α) sandwich/β-sandwich
|-
|'''Mechanism'''
|serine hydrolase
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE20.html
|}
</div>


== Substrate specificities ==
Carbohydrate esterase family 20 (CE20) currently comprises xyloglucan acetylesterases <cite>Vieira2021</cite> and acetylesterases putatively related to arabinoxylan deacetylation <cite>Liu2022</cite> .

== Kinetics and Mechanism ==
''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad (Asp-His-Ser). Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE1]]. However, this assumption still requires experimental validation. ''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 <cite>Vieira2021</cite>. Kinetic data for the second characterized member of family CE20, XuaJ, is available for the substrate 1-Naphthyl acetate <cite>Liu2022</cite>.

== Catalytic Residues ==
The founding members of this family seem to have the canonical catalytic triad (Asp-His-Ser) found in esterases from other families <cite>Vieira2021</cite>, but this inference still requires experimental validation.

== Three-dimensional structures ==
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 <cite>Vieira2021</cite>. Such structural architecture diverges from carbohydrate esterase (CE) families described in the CAZy database so far. In XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, 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 <cite>Cantarel2009 DaviesSinnott2008</cite>) in the α5-η3 loop .

== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
;First catalytic nucleophile identification: Content is to be added here.
;First general acid/base residue identification: Content is to be added here.

;First biochemical characterization: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase in 2021 <cite>Vieira2021</cite>.

;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 <cite>Vieira2021</cite>.
== References ==
<biblio>
#Cantarel2009 pmid=18838391
#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].

#Vieira2021 pmid=34193873

#Liu2022 pmid=36403068

</biblio>

[[Category:Carbohydrate Esterase Families|CE020]]

Carbohydrate Esterase Family 20

2023-03-22T17:24:42Z

Priscila Giuseppe:

{{UnderConstruction}}
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE20'''
|-
|'''Fold'''
|β-sandwich/(α-β-α) sandwich/β-sandwich
|-
|'''Mechanism'''
|serine hydrolase
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE20.html
|}
</div>


== Substrate specificities ==
Carbohydrate esterase family 20 (CE20) currently comprises xyloglucan acetylesterases <cite>Vieira2021</cite> and acetylesterases putatively related to arabinoxylan deacetylation <cite>Liu2022</cite> .

== Kinetics and Mechanism ==
''Xac''XaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad (Asp-His-Ser). Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE1]]. However, this assumption still requires experimental validation. XacXaeA 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 <cite>Vieira2021</cite>. Kinetic data for the second characterized member of family CE20 is available for the substrate 1-Naphthyl acetate <cite>Liu2022</cite>.

== Catalytic Residues ==
The founding members of this family seem to have the canonical catalytic triad (Asp-His-Ser) found in esterases from other families <cite>Vieira2021</cite>, but this inference still requires experimental validation.

== Three-dimensional structures ==
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 <cite>Vieira2021</cite>. Such structural architecture diverges from carbohydrate esterase (CE) families described in the CAZy database so far. In XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, 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 <cite>Cantarel2009 DaviesSinnott2008</cite>) in the α5-η3 loop .

== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
;First catalytic nucleophile identification: Content is to be added here.
;First general acid/base residue identification: Content is to be added here.
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 <cite>Vieira2021</cite>.

== References ==
<biblio>
#Cantarel2009 pmid=18838391
#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].

#Vieira2021 pmid=34193873

#Liu2022 pmid=36403068

</biblio>

[[Category:Carbohydrate Esterase Families|CE020]]

Carbohydrate Esterase Family 20

2023-03-22T17:17:18Z

Priscila Giuseppe:

{{UnderConstruction}}
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE20'''
|-
|'''Fold'''
|β-sandwich/(α-β-α) sandwich/β-sandwich
|-
|'''Mechanism'''
|serine hydrolase
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE20.html
|}
</div>


== Substrate specificities ==
Carbohydrate esterase family 20 (CE20) currently comprises xyloglucan acetylesterases <cite>Vieira2021</cite> and acetylesterases putatively related to arabinoxylan deacetylation <cite>Liu2022</cite> .

== Kinetics and Mechanism ==
XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad (Asp-His-Ser). Thus, it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE1]]. However, this assumption still requires experimental validation.

== Catalytic Residues ==
The caracterized members of this family seem to have the canonical catalytic triad (Asp-His-Ser) found in esterases from other families, but this inference still requires experimental validation.

== Three-dimensional structures ==
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 <cite>Vieira2021</cite>. Such structural architecture diverges from carbohydrate esterase (CE) families described in the CAZy database so far. In XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, 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 <cite>Cantarel2009 DaviesSinnott2008</cite>) in the α5-η3 loop .

== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
;First catalytic nucleophile identification: Content is to be added here.
;First general acid/base residue identification: Content is to be added here.
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 <cite>Vieira2021</cite>.

== References ==
<biblio>
#Cantarel2009 pmid=18838391
#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].

#Vieira2021 pmid=34193873

#Liu2022 pmid=36403068

</biblio>

[[Category:Carbohydrate Esterase Families|CE020]]

Carbohydrate Esterase Family 20

2023-03-22T17:12:53Z

Priscila Giuseppe:

{{UnderConstruction}}
* [[Author]]s: [[User:Plinio Vieira|Plinio Salmazo Vieira]] and [[User:Priscila Giuseppe|Priscila Oliveira Giuseppe]]
* [[Responsible Curator]]: [[User:Mario Murakami|Mario Murakami]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE20'''
|-
|'''Fold'''
|β-sandwich/(α-β-α) sandwich/β-sandwich
|-
|'''Mechanism'''
|serine hydrolase
|-
|'''Active site residues'''
|known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CE20.html
|}
</div>


== Substrate specificities ==
Carbohydrate esterase family 20 (CE20) currently comprises xyloglucan acetylesterases <cite>Vieira2021</cite> and acetylesterases putatively related to arabinoxylan deacetylation <cite>Liu2022</cite> .

== Kinetics and Mechanism ==
Content is to be added here.

== Catalytic Residues ==
XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, harbors the canonical catalytic triad (Asp-His-Ser). Thus it is supposed to have the same mechanism of action described for other carbohydrate esterases, such as the members of family [[CE1]]. However, this assumption still requires experimental validation.

== Three-dimensional structures ==
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 <cite>Vieira2021</cite>. Such structural architecture diverges from carbohydrate esterase (CE) families described in the CAZy database so far. In XacXaeA, the founding member of family CE20 <cite>Vieira2021</cite>, 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 <cite>Cantarel2009</cite>) in the α5-η3 loop .

== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
;First catalytic nucleophile identification: Content is to be added here.
;First general acid/base residue identification: Content is to be added here.
;First 3-D structure: ''Xanthomonas citri'' subsp. ''citri'' 306 xyloglucan acetylesterase crystal structure in 2021 <cite>Vieira2021</cite>.

== References ==
<biblio>
#Cantarel2009 pmid=18838391
#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].

#Vieira2021 pmid=34193873

#Liu2022 pmid=36403068

</biblio>

[[Category:Carbohydrate Esterase Families|CE020]]

Carbohydrate Esterase Family 20

2023-03-22T15:22:54Z

Priscila Giuseppe:

User:Priscila Giuseppe

2023-03-22T14:02:25Z

Priscila Giuseppe:

[[Image:pgiuseppe.jpg|200px|right]]

Priscila Giuseppe earned a B.Sc. in Biological Sciences from the State University of Campinas and a PhD in Protein X-ray Crystallography from the Graduate Program in Genetics and Molecular Biology at the same university. Her doctoral research was conducted at [https://cnpem.br/ CNPEM] (Brazil) and Synchrotron Soleil (France), under the supervision of Beatriz Guimarães, and at the Institut Pasteur (France) under the supervision of Mathieu Picardeau. In 2011, she joined the group of
[[User:Mario Murakami|Mario Murakami]], as a research associate at the [https://lnbio.cnpem.br/ Brazilian Biosciences National Laboratory (LNBio-CNPEM)], contributing on several studies on the molecular mechanisms that drive protein function and biocatalysis. Since 2020 she has been a Principal Investigator at the [ https://lnbr.cnpem.br/ Brazilian Biorenewables National Laboratory], leading a research group focused on the study and development of biocatalytic strategies for lignin valorization.
In the glycobiology field, she has contributed to structural and functional studies related to members of the following CAZy families:

*[[GH1]] HiBG <cite>Giuseppe2014</cite> and ''Ea''BglA <cite>Zanphorlin2016</cite>

*[[GH3]] ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C <cite>Vieira2021</cite>

*[[GH5]] subfamily 18 ''Bl''Man5B <cite>Cordeiro2019</cite>

*[[GH8]] ''Xac''Cel8 <cite>Melo2021</cite>

*[[GH31]] ''Xac''Xyl31 <cite>Vieira2021</cite> and Bl_Glc31 <cite>Cordeiro2023</cite>

*[[GH35]] ''Xac''GalD <cite>Vieira2021</cite>

*[[GH38]] Bl_Man38A, Bl_Man38B, Bl_Man38C <cite>Cordeiro2023</cite>

*[[GH51]] ''Xac''Abf51 <cite>Santos2018</cite>

*[[GH74]] ''Xac''Xeg74 <cite>Vieira2021</cite>

*[[GH85]] Bl_Endo85 <cite>Cordeiro2023</cite>

*[[GH95]] ''Xac''Afc95 <cite>Vieira2021</cite>

*[[GH125]] Bl_Man125 <cite>Cordeiro2023</cite>

*[[CE20]] ''Xac''XaeA <cite>Vieira2021</cite>

----
<biblio>
#Giuseppe2014 pmid=24914974
#Zanphorlin2016 pmid=27029646
#Vieira2021 pmid=34193873
#Cordeiro2019 pmid=30641082
#Melo2021 pmid=33164774
#Cordeiro2023 pmid=36443572
#Santos2018 pmid=30127853

</biblio>


[[Category:Contributors|Giuseppe,Priscila]]

User:Priscila Giuseppe

2023-03-22T14:00:48Z

Priscila Giuseppe:

[[Image:pgiuseppe.jpg|200px|right]]

Priscila Giuseppe earned a B.Sc. in Biological Sciences from the State University of Campinas and a PhD in Protein X-ray Crystallography from the Graduate Program in Genetics and Molecular Biology at the same university. Her doctoral research was conducted at [https://cnpem.br/ CNPEM] (Brazil) and Synchrotron Soleil (France), under the supervision of Beatriz Guimarães, and at the Institut Pasteur (France) under the supervision of Mathieu Picardeau. In 2011, she joined the group of
[[User:Mario Murakami|Mario Murakami]], as a research associate at the [https://lnbio.cnpem.br/ Brazilian Biosciences National Laboratory (LNBio-CNPEM)], contributing on several studies on the molecular mechanisms that drive protein function and biocatalysis. Since 2020 she has been a Principal Investigator at the [ https://lnbr.cnpem.br/ Brazilian Biorenewables National Laboratory], leading a research group focused on the study and development of biocatalytic strategies for lignin valorization.
In the glycobiology field, she has contributed to structural and functional studies related to members of the following CAZy families:

*[[GH1]] HiBG <cite>Giuseppe2014</cite> and ''Ea''BglA <cite>Zanphorlin2016</cite>

*[[GH3]] ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C <cite>Vieira2021</cite>

*[[GH5]] subfamily 18 ''Bl''Man5B <cite>Cordeiro2019</cite>

*[[GH8]] ''Xac''Cel8 <cite>Melo2021</cite>

*[[GH31]] ''Xac''Xyl31 <cite>Vieira2021</cite> and Bl_Glc31 <cite>Cordeiro2023</cite>

*[[GH35]] ''Xac''GalD <cite>Vieira2021</cite>

*[[GH38]] Bl_Man38A, Bl_Man38B, Bl_Man38C <cite>Cordeiro2023</cite>

*[[GH51]] ''Xac''Abf51 <cite>Santos2018</cite>

*[[GH74]] ''Xac''Xeg74 <cite>Vieira2021</cite>

*[[GH85]] Bl_Endo85 <cite>Cordeiro2023</cite>

*[[GH95]] ''Xac''Afc95 <cite>Vieira2021</cite>

*[[GH125]] Bl_Man125 <cite>Cordeiro2023</cite>

*[[CE20]] ''Xac''XaeA <cite>Vieira2021</cite>
----

<biblio>
#Giuseppe2014 pmid=24914974
#Zanphorlin2016 pmid=27029646
#Vieira2021 pmid=34193873
#Cordeiro2019 pmid=30641082
#Melo2021 pmid=33164774
#Cordeiro2023 pmid=36443572
#Santos2018 pmid=30127853

</biblio>


[[Category:Contributors|Giuseppe,Priscila]]

File:Pgiuseppe.jpg

2023-03-22T13:59:51Z

Priscila Giuseppe: Priscila Giuseppe

== Summary ==
Priscila Giuseppe

User:Priscila Giuseppe

2023-03-22T13:54:25Z

Priscila Giuseppe:

[[Image:Blank_user-200px.png|200px|right]]

Priscila Giuseppe earned a B.Sc. in Biological Sciences from the State University of Campinas and a PhD in Protein X-ray Crystallography from the Graduate Program in Genetics and Molecular Biology at the same university. Her doctoral research was conducted at [https://cnpem.br/ CNPEM] (Brazil) and Synchrotron Soleil (France), under the supervision of Beatriz Guimarães, and at the Institut Pasteur (France) under the supervision of Mathieu Picardeau. In 2011, she joined the group of
[[User:Mario Murakami|Mario Murakami]], as a research associate at the [https://lnbio.cnpem.br/ Brazilian Biosciences National Laboratory (LNBio-CNPEM)], contributing on several studies on the molecular mechanisms that drive protein function and biocatalysis. Since 2020 she has been a Principal Investigator at the [ https://lnbr.cnpem.br/ Brazilian Biorenewables National Laboratory], leading a research group focused on the study and development of biocatalytic strategies for lignin valorization.
In the glycobiology field, she has contributed to structural and functional studies related to members of the following CAZy families:

*[[GH1]] HiBG <cite>Giuseppe2014</cite> and ''Ea''BglA <cite>Zanphorlin2016</cite>

*[[GH3]] ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C <cite>Vieira2021</cite>

*[[GH5]] subfamily 18 ''Bl''Man5B <cite>Cordeiro2019</cite>

*[[GH8]] ''Xac''Cel8 <cite>Melo2021</cite>

*[[GH31]] ''Xac''Xyl31 <cite>Vieira2021</cite> and Bl_Glc31 <cite>Cordeiro2023</cite>

*[[GH35]] ''Xac''GalD <cite>Vieira2021</cite>

*[[GH38]] Bl_Man38A, Bl_Man38B, Bl_Man38C <cite>Cordeiro2023</cite>

*[[GH51]] ''Xac''Abf51 <cite>Santos2018</cite>

*[[GH74]] ''Xac''Xeg74 <cite>Vieira2021</cite>

*[[GH85]] Bl_Endo85 <cite>Cordeiro2023</cite>

*[[GH95]] ''Xac''Afc95 <cite>Vieira2021</cite>

*[[GH125]] Bl_Man125 <cite>Cordeiro2023</cite>

*[[CE20]] ''Xac''XaeA <cite>Vieira2021</cite>
----

<biblio>
#Giuseppe2014 pmid=24914974
#Zanphorlin2016 pmid=27029646
#Vieira2021 pmid=34193873
#Cordeiro2019 pmid=30641082
#Melo2021 pmid=33164774
#Cordeiro2023 pmid=36443572
#Santos2018 pmid=30127853

</biblio>


[[Category:Contributors|Giuseppe,Priscila]]