https://www.cazypedia.org/api.php?action=feedcontributions&user=Casper+Wilkens&feedformat=atomCAZypedia - User contributions [en-ca]2024-03-28T17:01:14ZUser contributionsMediaWiki 1.35.10https://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_6&diff=16309Carbohydrate Esterase Family 62021-10-09T13:52:27Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE6'''<br />
|-<br />
|'''Fold''' <br />
|( α / β / α)-sandwich<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE6.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]) - an activity also found in families [[CE2]], [[CE3]], [[CE4]], [[CE5]], [[CE7]], and [[CE12]] <cite>Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE6 acetyl xylan esterases target the 2-, 3- or 2,3-linked ''O''-acetyl substituents on the β-1,4-linked xylopyranosyl moieties that comprise the xylan backbone.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: ''Arabidopsis thaliana apo'' acetyl xylan esterase in 2005 [https://www.rcsb.org/structure/2APJ PDB ID 2APJ] <cite>Bitto2005</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Cantarel2009 pmid=18838391<br />
<br />
#Bitto2005 pmid=16301800<br />
<br />
#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].<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE006]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_6&diff=16308Carbohydrate Esterase Family 62021-10-09T13:47:20Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE6'''<br />
|-<br />
|'''Fold''' <br />
|( α / β / α)-sandwich<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE6.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]) - an activity also found in [[CE2]], [[CE3]], [[CE4]], [[CE5]], [[CE7]], and [[CE12]] <cite>Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: ''Arabidopsis thaliana apo'' acetyl xylan esterase in 2005 [https://www.rcsb.org/structure/2APJ PDB ID 2APJ] <cite>Bitto2005</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Cantarel2009 pmid=18838391<br />
<br />
#Bitto2005 pmid=16301800<br />
<br />
#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].<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE006]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_6&diff=16307Carbohydrate Esterase Family 62021-10-09T13:46:27Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE6'''<br />
|-<br />
|'''Fold''' <br />
|( α / β / α)-sandwich<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE6.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]) - an activity also found in [[CE2]], CE3, CE4, CE5, CE7, and CE12 <cite>Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: ''Arabidopsis thaliana apo'' acetyl xylan esterase in 2005 [https://www.rcsb.org/structure/2APJ PDB ID 2APJ] <cite>Bitto2005</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Cantarel2009 pmid=18838391<br />
<br />
#Bitto2005 pmid=16301800<br />
<br />
#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].<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE006]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_6&diff=16306Carbohydrate Esterase Family 62021-10-09T13:40:12Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE6'''<br />
|-<br />
|'''Fold''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE6.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]) <cite>Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: ''Arabidopsis thaliana apo'' acetyl xylan esterase in 2005 [https://www.rcsb.org/structure/2APJ PDB ID 2APJ] <cite>Bitto2005</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Cantarel2009 pmid=18838391<br />
<br />
#Bitto2005 pmid=16301800<br />
<br />
#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].<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE006]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_6&diff=16305Carbohydrate Esterase Family 62021-10-09T13:39:44Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE6'''<br />
|-<br />
|'''Fold''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE6.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]) <cite>Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: ''Arabidopsis thaliana'' acetyl xylan esterase in 2005 [https://www.rcsb.org/structure/2APJ PDB ID 2APJ] <cite>Bitto2005</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Cantarel2009 pmid=18838391<br />
<br />
#Bitto2005 pmid=16301800<br />
<br />
#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].<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE006]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_6&diff=16304Carbohydrate Esterase Family 62021-10-09T13:38:48Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE6'''<br />
|-<br />
|'''Fold''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE6.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]) <cite>Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: ''Arabidopsis thaliana'' acetyl xylan esterase in 2005 [https://www.rcsb.org/structure/2APJ PDB ID 2APJ] <cite>X</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Cantarel2009 pmid=18838391<br />
<br />
#Bitto2005 pmid=16301800<br />
<br />
#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].<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE006]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=16221User:Casper Wilkens2021-04-09T08:58:01Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Casper-Wilkens.jpg|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third Post Doc at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
----<br />
<br />
<biblio><br />
<br />
#Pilgaard2021 pmid=33503820<br />
#Qiu2020 pmid=32768519<br />
<br />
#Holck2019b pmid=31558605<br />
<br />
#Pilgaard2019a pmid=31451726<br />
<br />
#Holck2019a pmid=31307573<br />
#Wilkens2019a pmid=30315603<br />
#Wilkens2018a pmid=30483298<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=16220User:Casper Wilkens2021-04-09T08:57:48Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Casper-Wilkens.jpg|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third Post Doc at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
<br />
#Pilgaard2021 pmid=33503820<br />
#Qiu2020 pmid=32768519<br />
<br />
#Holck2019b pmid=31558605<br />
<br />
#Pilgaard2019a pmid=31451726<br />
<br />
#Holck2019a pmid=31307573<br />
#Wilkens2019a pmid=30315603<br />
#Wilkens2018a pmid=30483298<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=16219User:Casper Wilkens2021-04-09T08:56:40Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Casper-Wilkens.jpg|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third post at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
<br />
#Pilgaard2021 pmid=33503820<br />
#Qiu2020 pmid=32768519<br />
<br />
#Holck2019b pmid=31558605<br />
<br />
#Pilgaard2019a pmid=31451726<br />
<br />
#Holck2019a pmid=31307573<br />
#Wilkens2019a pmid=30315603<br />
#Wilkens2018a pmid=30483298<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=File:Casper-Wilkens.jpg&diff=16218File:Casper-Wilkens.jpg2021-04-09T08:53:56Z<p>Casper Wilkens: Casper Wilkens profil picture</p>
<hr />
<div>Casper Wilkens profil picture</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=16217User:Casper Wilkens2021-04-09T08:45:36Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third post at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
<br />
#Pilgaard2021 pmid=33503820<br />
#Qiu2020 pmid=32768519<br />
<br />
#Holck2019b pmid=31558605<br />
<br />
#Pilgaard2019a pmid=31451726<br />
<br />
#Holck2019a pmid=31307573<br />
#Wilkens2019a pmid=30315603<br />
#Wilkens2018a pmid=30483298<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_6&diff=15215Carbohydrate Esterase Family 62020-06-06T12:39:16Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE6'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE6.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]) <cite>Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#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].<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE006]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_6&diff=15214Carbohydrate Esterase Family 62020-06-06T12:38:58Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^<br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family CE6'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE6.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 6 (CE6) comprises only acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72])<cite>Cantarel2009</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: Content is to be added here.<br />
<br />
== References ==<br />
<biblio><br />
#Cantarel2009 pmid=18838391<br />
#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].<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE006]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14798Carbohydrate Esterase Family 12020-05-06T13:18:26Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^ <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|α/β/α-sandwich<br />
|-<br />
|'''Mechanism'''<br />
|serine hydrolase<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, all appear to utilize the canonical serine hydrolase mechanism, involving a catalytic triad comprising a nucleophilic serine, a histidine, and an acidic amino acid <cite>Schubot2001 Prates2001</cite>. Both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite>. After substrate binding, the serine is activated by the proton relay consisting of the histidine and the acid residue, which facilitates nucleophilic attack of the carbonyl carbon atom of the substrate. This results in the formation of a covalent acyl-enzyme intermediate via a tetrahedral transition state (sometimes known as the "tetrahedral intermediate"), which is stabilized through interactions with two main-chain NH groups in the "oxyanion hole." Following release of the corresponding alcohol as the first product, the acyl-enzyme intermediate is hydrolyzed by the near-microscopic reverse of the first step, with water, activated by the proton relay, acting as the nucleophile <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The catalytic serine is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called "nucleophilic elbow", which serves as a fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine is also conserved <cite>Schubot2001 Prates2001</cite>, while the [[general acid]] may be an aspartic acid or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1 is a member of the α/β-hydrolase superfamily <cite>Ronning2000</cite> or refered to as an α/β/α-sandwich, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. A number of CE1 feruloyl esterases have a [[CBM48]] appended that proved to be essential for feruloyl esterase activity on polymeric xylan <cite>Holck2019</cite>, however, there are examples of CE1 feruloyl esterases lacking a CBM that act on polymeric xylan <cite>Wefers2017</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Experiments performed at DSM N. V. published in a patent application in 1992 [https://patents.google.com/patent/EP0507369A2/en EP0507369A2 ]showed that an enzyme from '' Trichoderma reesei '' later on classified as a CE1 enzyme was able to deacetylate xylans. Prior to the sequence published in the patent [https://patents.google.com/patent/EP0507369A2/en EP0507369A2] several papers reported on the characterization of native acetylxylan esterases purified from ''T. reesei'' ([https://link.springer.com/article/10.1007/BF00172542 Poutanen et al. 1990];[https://www.nrcresearchpress.com/doi/abs/10.1139/m88-130 Biely et al. 1988]). In 2000 more comprehensive characterizations than in above mentioned patent of two CE1 enzymes were published for a cinnamoyl esterase from ''Penicillium funiculosum'' <cite>Kroon2000</cite> and a mycolyltransferase from ''Mycobacterium'' ''tuberculosis'' <cite>Ronning2000</cite>. <br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
#Holck2019 pmid=31558605<br />
#Kroon2000 pmid=11082184<br />
#Wefers2017 pmid=28669823</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14797Carbohydrate Esterase Family 12020-05-06T13:17:07Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^ <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|α/β/α-sandwich<br />
|-<br />
|'''Mechanism'''<br />
|serine hydrolase<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, all appear to utilize the canonical serine hydrolase mechanism, involving a catalytic triad comprising a nucleophilic serine, a histidine, and an acidic amino acid <cite>Schubot2001 Prates2001</cite>. Both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite>. After substrate binding, the serine is activated by the proton relay consisting of the histidine and the acid residue, which facilitates nucleophilic attack of the carbonyl carbon atom of the substrate. This results in the formation of a covalent acyl-enzyme intermediate via a tetrahedral transition state (sometimes known as the "tetrahedral intermediate"), which is stabilized through interactions with two main-chain NH groups in the "oxyanion hole." Following release of the corresponding alcohol as the first product, the acyl-enzyme intermediate is hydrolyzed by the near-microscopic reverse of the first step, with water, activated by the proton relay, acting as the nucleophile <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The catalytic serine is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called "nucleophilic elbow", which serves as a fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine is also conserved <cite>Schubot2001 Prates2001</cite>, while the [[general acid]] may be an aspartic acid or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1 is a member of the α/β-hydrolase superfamily <cite>Ronning2000</cite> or refered to as an α/β/α-sandwich, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. A number of CE1 feruloyl esterases have a [[CBM48]] appended that proved to be essential for feruloyl esterase activity on polymeric xylan <cite>Holck2019</cite>, however, there are examples of CE1 feruloyl esterases lacking a CBM that act on polymeric xylan <cite>Wefers2017</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Experiments performed at DSM N. V. published in a patent application in 1992 [https://patents.google.com/patent/EP0507369A2/en EP0507369A2 ]showed that an enzyme from '' Trichoderma reesei '' later on classified as a CE1 enzyme was able to deacetylate xylans. Prior to the sequence published in the patent [https://patents.google.com/patent/EP0507369A2/en EP0507369A2] several papers reported on the characterization of native acetylxylan esterases purified from ''T. reesei'' ([https://link.springer.com/article/10.1007/BF00172542 Poutanen et al. 1990];[https://www.nrcresearchpress.com/doi/abs/10.1139/m88-130 Biely et al. 1988]). In 2000 a more comprehensive characterization than in above mentioned patent of two CE1 enzymes were published – a cinnamoyl esterase from ''Penicillium funiculosum'' <cite>Kroon2000</cite> and a mycolyltransferase from ''Mycobacterium'' ''tuberculosis'' <cite>Ronning2000</cite>. <br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
#Holck2019 pmid=31558605<br />
#Kroon2000 pmid=11082184<br />
#Wefers2017 pmid=28669823</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14796Carbohydrate Esterase Family 12020-05-06T13:16:18Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^ <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|α/β/α-sandwich<br />
|-<br />
|'''Mechanism'''<br />
|serine hydrolase<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, all appear to utilize the canonical serine hydrolase mechanism, involving a catalytic triad comprising a nucleophilic serine, a histidine, and an acidic amino acid <cite>Schubot2001 Prates2001</cite>. Both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite>. After substrate binding, the serine is activated by the proton relay consisting of the histidine and the acid residue, which facilitates nucleophilic attack of the carbonyl carbon atom of the substrate. This results in the formation of a covalent acyl-enzyme intermediate via a tetrahedral transition state (sometimes known as the "tetrahedral intermediate"), which is stabilized through interactions with two main-chain NH groups in the "oxyanion hole." Following release of the corresponding alcohol as the first product, the acyl-enzyme intermediate is hydrolyzed by the near-microscopic reverse of the first step, with water, activated by the proton relay, acting as the nucleophile <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The catalytic serine is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called "nucleophilic elbow", which serves as a fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine is also conserved <cite>Schubot2001 Prates2001</cite>, while the [[general acid]] may be an aspartic acid or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1 is a member of the α/β-hydrolase superfamily <cite>Ronning2000</cite> or refered to as an α/β/α-sandwich, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. A number of CE1 feruloyl esterases have a [[CBM48]] appended that proved to be essential for feruloyl esterase activity on polymeric xylan <cite>Holck2019</cite>, however, there are examples of CE1 feruloyl esterases lacking a CBM that act on polymeric xylan <cite>Wefers2017</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Experiments performed at DSM N. V. published in a patent application in 1992 [https://patents.google.com/patent/EP0507369A2/en EP0507369A2 ]showed that an enzyme from '' Trichoderma reesei '' later on classified as a CE1 enzyme was able to deacetylate xylans. Prior to the sequence published in the patent [https://patents.google.com/patent/EP0507369A2/en EP0507369A2] several papers reported on the characterization of native xylan acetyl esterases purified from ''T. reesei'' ([https://link.springer.com/article/10.1007/BF00172542 Poutanen et al. 1990];[https://www.nrcresearchpress.com/doi/abs/10.1139/m88-130 Biely et al. 1988]). In 2000 a more comprehensive characterization than in above mentioned patent of two CE1 enzymes were published – a cinnamoyl esterase from ''Penicillium funiculosum'' <cite>Kroon2000</cite> and a mycolyltransferase from ''Mycobacterium'' ''tuberculosis'' <cite>Ronning2000</cite>. <br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
#Holck2019 pmid=31558605<br />
#Kroon2000 pmid=11082184<br />
#Wefers2017 pmid=28669823</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14795Carbohydrate Esterase Family 12020-05-06T13:15:37Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^ <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|α/β/α-sandwich<br />
|-<br />
|'''Mechanism'''<br />
|serine hydrolase<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, all appear to utilize the canonical serine hydrolase mechanism, involving a catalytic triad comprising a nucleophilic serine, a histidine, and an acidic amino acid <cite>Schubot2001 Prates2001</cite>. Both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite>. After substrate binding, the serine is activated by the proton relay consisting of the histidine and the acid residue, which facilitates nucleophilic attack of the carbonyl carbon atom of the substrate. This results in the formation of a covalent acyl-enzyme intermediate via a tetrahedral transition state (sometimes known as the "tetrahedral intermediate"), which is stabilized through interactions with two main-chain NH groups in the "oxyanion hole." Following release of the corresponding alcohol as the first product, the acyl-enzyme intermediate is hydrolyzed by the near-microscopic reverse of the first step, with water, activated by the proton relay, acting as the nucleophile <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The catalytic serine is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called "nucleophilic elbow", which serves as a fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine is also conserved <cite>Schubot2001 Prates2001</cite>, while the [[general acid]] may be an aspartic acid or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1 is a member of the α/β-hydrolase superfamily <cite>Ronning2000</cite> or refered to as an α/β/α-sandwich, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. A number of CE1 feruloyl esterases have a [[CBM48]] appended that proved to be essential for feruloyl esterase activity on polymeric xylan <cite>Holck2019</cite>, however, there are examples of CE1 feruloyl esterases lacking a CBM that act on polymeric xylan <cite>Wefers2017</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Experiments performed at DSM N. V. published in a patent application in 1992 [https://patents.google.com/patent/EP0507369A2/en EP0507369A2 ]showed that an enzyme from '' Trichoderma reesei '' later on classified as a CE1 enzyme was able to deacetylate xylans. Prior to the sequence published in the patent [https://patents.google.com/patent/EP0507369A2/en EP0507369A2] several papers reported on the characterization of native xylan acetyl esterases purified from ''T. reesei'' [https://link.springer.com/article/10.1007/BF00172542 Poutanen et al. 1990][https://www.nrcresearchpress.com/doi/abs/10.1139/m88-130 Biely et al. 1988]. In 2000 a more comprehensive characterization than in above mentioned patent of two CE1 enzymes were published – a cinnamoyl esterase from ''Penicillium funiculosum'' <cite>Kroon2000</cite> and a mycolyltransferase from ''Mycobacterium'' ''tuberculosis'' <cite>Ronning2000</cite>. <br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
#Holck2019 pmid=31558605<br />
#Kroon2000 pmid=11082184<br />
#Wefers2017 pmid=28669823</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14794Carbohydrate Esterase Family 12020-05-05T11:49:13Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^ <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|α/β/α-sandwich<br />
|-<br />
|'''Mechanism'''<br />
|serine hydrolase<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, all appear to utilize the canonical serine hydrolase mechanism, involving a catalytic triad comprising a nucleophilic serine, a histidine, and an acidic amino acid <cite>Schubot2001 Prates2001</cite>. Both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite>. After substrate binding, the serine is activated by the proton relay consisting of the histidine and the acid residue, which facilitates nucleophilic attack of the carbonyl carbon atom of the substrate. This results in the formation of a covalent acyl-enzyme intermediate via a tetrahedral transition state (sometimes known as the "tetrahedral intermediate"), which is stabilized through interactions with two main-chain NH groups in the "oxyanion hole." Following release of the corresponding alcohol as the first product, the acyl-enzyme intermediate is hydrolyzed by the near-microscopic reverse of the first step, with water, activated by the proton relay, acting as the nucleophile <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The catalytic serine is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called "nucleophilic elbow", which serves as a fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine is also conserved <cite>Schubot2001 Prates2001</cite>, while the [[general acid]] may be an aspartic acid or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1 is a member of the α/β-hydrolase superfamily <cite>Ronning2000</cite> or refered to as an α/β/α-sandwich, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. A number of CE1 feruloyl esterases have a [[CBM48]] appended that proved to be essential for feruloyl esterase activity on polymeric xylan <cite>Holck2019</cite>, however, there are examples of CE1 feruloyl esterases lacking a CBM that act on polymeric xylan <cite>Wefers2017</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
#Holck2019 pmid=31558605<br />
<br />
#Wefers2017 pmid=28669823</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14770Carbohydrate Esterase Family 12020-04-20T06:15:51Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^ <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|α/β-hydrolase superfamily<br />
|-<br />
|'''Mechanism'''<br />
|serine hydrolase<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, all appear to utilize the canonical serine hydrolase mechanism, involving a catalytic triad comprising a nucleophilic serine, a histidine, and an acidic amino acid <cite>Schubot2001 Prates2001</cite>. Both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite>. After substrate binding, the serine is activated by the proton relay consisting of the histidine and the acid residue, which facilitates nucleophilic attack of the carbonyl carbon atom of the substrate. This results in the formation of a covalent acyl-enzyme intermediate via a tetrahedral transition state (sometimes known as the "tetrahedral intermediate"), which is stabilized through interactions with two main-chain NH groups in the "oxyanion hole." Following release of the corresponding alcohol as the first product, the acyl-enzyme intermediate is hydrolyzed by the near-microscopic reverse of the first step, with water, activated by the proton relay, acting as the nucleophile <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The catalytic serine is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called "nucleophilic elbow", which serves as a fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine is also conserved <cite>Schubot2001 Prates2001</cite>, while the [[general acid]] may be an aspartic acid or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1 is a member of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. A number of CE1 feruloyl esterases have a [[CBM48]] appended that proved to be essential for feruloyl esterase activity on polymeric xylan <cite>Holck2019</cite>, however, there are examples of CE1 feruloyl esterases lacking a CBM that act on polymeric xylan <cite>Wefers2017</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
#Holck2019 pmid=31558605<br />
<br />
#Wefers2017 pmid=28669823</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14769Carbohydrate Esterase Family 12020-04-20T06:15:18Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: ^^^Harry Brumer^^^ <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|α/β-hydrolase superfamily<br />
|-<br />
|'''Mechanism'''<br />
|serine hydrolase<br />
|-<br />
|'''Active site residues'''<br />
|known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, all appear to utilize the canonical serine hydrolase mechanism, involving a catalytic triad comprising a nucleophilic serine, a histidine, and an acidic amino acid <cite>Schubot2001 Prates2001</cite>. Both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite>. After substrate binding, the serine is activated by the proton relay consisting of the histidine and the acid residue, which facilitates nucleophilic attack of the carbonyl carbon atom of the substrate. This results in the formation of a covalent acyl-enzyme intermediate via a tetrahedral transition state (sometimes known as the "tetrahedral intermediate"), which is stabilized through interactions with two main-chain NH groups in the "oxyanion hole." Following release of the corresponding alcohol as the first product, the acyl-enzyme intermediate is hydrolyzed by the near-microscopic reverse of the first step, with water, activated by the proton relay, acting as the nucleophile <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The catalytic serine is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called "nucleophilic elbow", which serves as a fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine is also conserved <cite>Schubot2001 Prates2001</cite>, while the [[general acid]] may be an aspartic acid or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1 is a member of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. A number of CE1 feruloyl esterases have a [[CBM48]] appended that proved to be essential for feruloyl esterase activity on polymeric xylan <cite>Holck2019</cite>, however, there are examples of CE1 feruloyl esterases lacking a CBM, which act on polymeric xylan <cite>Wefers2017</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
#Holck2019 pmid=31558605<br />
<br />
#Wefers2017 pmid=28669823</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14609Carbohydrate Esterase Family 12020-03-23T10:55:55Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, the general mechanism of hydrolysis, involving the serine [[general base]], a histidine acting as general acid-base catalyst, and a [[general acid]], appears to be conserved <cite>Schubot2001 Prates2001</cite>. The [[general acid]] is structurally conserved, but both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite> After substrate binding, the serine is activated by the histidine, which allows the nucleophilic attack of the substrate’s carbonyl carbon atom leading to the formation of a covalent acyl-enzyme intermediate via tetrahedral transition states sometimes known as the “tetrahedral intermediates.” Simultaneously, a proton is transferred from the serine to the histidine. The resulting tetrahydral intermediate, negatively charged carbonyl oxygen atom (“oxyanion”) is stabilized through interactions with two main chain NH groups in the “oxyanion hole”, while the positively charged histidine is stabilized by a hydrogen bond to the catalytic acid. In the next step, the formed alcohol is released from the substrate and the acid part forms an ester bond with the serine oxygen. This bond, in turn, is hydrolyzed in a two- step mechanism involving a water molecule, and the enzyme is returned to the starting point <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The serine [[general base]] is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called “nucleophilic elbow”, which has become the fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine acting as general acid-base catalyst is also conserved <cite>Schubot2001 Prates2001</cite>, while the [[general acid]] commonly is observed as both a aspartic or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. A number of CE1 enzymes have a [[CBM48]] appended, which proved to be essential for these feruloyl esterases acticity on polymeric xylan <cite>Holck2019</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lombard2014 pmid=24270786<br />
<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
<br />
#Holck2019 pmid=31558605<br />
<br />
</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14608Carbohydrate Esterase Family 12020-03-23T10:54:30Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, the general mechanism of hydrolysis, involving the serine ([[general base]]), a histidine acting as general acid-base catalyst, and a ([[general acid]]), appears to be conserved <cite>Schubot2001 Prates2001</cite>. The ([[general acid]]) is structurally conserved, but both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite> After substrate binding, the serine is activated by the histidine, which allows the nucleophilic attack of the substrate’s carbonyl carbon atom leading to the formation of a covalent acyl-enzyme intermediate via tetrahedral transition states sometimes known as the “tetrahedral intermediates.” Simultaneously, a proton is transferred from the serine to the histidine. The resulting tetrahydral intermediate, negatively charged carbonyl oxygen atom (“oxyanion”) is stabilized through interactions with two main chain NH groups in the “oxyanion hole”, while the positively charged histidine is stabilized by a hydrogen bond to the catalytic acid. In the next step, the formed alcohol is released from the substrate and the acid part forms an ester bond with the serine oxygen. This bond, in turn, is hydrolyzed in a two- step mechanism involving a water molecule, and the enzyme is returned to the starting point <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The serine ([[general base]]) is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called “nucleophilic elbow”, which has become the fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine acting as general acid-base catalyst is also conserved <cite>Schubot2001 Prates2001</cite>, while the ([[general acid]]) commonly is observed as both a aspartic or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. A number of CE1 enzymes have a [[CBM48]] appended, which proved to be essential for these feruloyl esterases acticity on polymeric xylan <cite>Holck2019</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lombard2014 pmid=24270786<br />
<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
<br />
#Holck2019 pmid=31558605<br />
<br />
</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14607Carbohydrate Esterase Family 12020-03-23T10:43:45Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, the general mechanism of hydrolysis, involving the serine general base, a histidine acting as general acid-base catalyst, and a general acid, appears to be conserved <cite>Schubot2001 Prates2001</cite>. The general acid is structurally conserved, but both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite> After substrate binding, the serine is activated by the histidine, which allows the nucleophilic attack of the substrate’s carbonyl carbon atom leading to the formation of a covalent acyl-enzyme intermediate via tetrahedral transition states sometimes known as the “tetrahedral intermediates.” Simultaneously, a proton is transferred from the serine to the histidine. The resulting tetrahydral intermediate, negatively charged carbonyl oxygen atom (“oxyanion”) is stabilized through interactions with two main chain NH groups in the “oxyanion hole”, while the positively charged histidine is stabilized by a hydrogen bond to the catalytic acid. In the next step, the formed alcohol is released from the substrate and the acid part forms an ester bond with the serine oxygen. This bond, in turn, is hydrolyzed in a two- step mechanism involving a water molecule, and the enzyme is returned to the starting point <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The serine genral base is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called “nucleophilic elbow”, which has become the fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine acting as general acid-base catalyst is also conserved <cite>Schubot2001 Prates2001</cite>, while the general acid commonly is observed as both a aspartic or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lombard2014 pmid=24270786<br />
<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
<br />
#Holck2019 pmid=31558605<br />
<br />
</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=14606Carbohydrate Esterase Family 12020-03-23T10:43:15Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, the general mechanism of hydrolysis, involving the serine general base, a histidine acting as general acid-base catalyst, and a general acid, appears to be conserved <cite>Schubot2001 Prates2001</cite>. The general acid is structurally conserved, but both aspartic and glutamic acid are commonly observed in the position <cite>Holck2019</cite> After substrate binding, the serine is activated by the histidine, which allows the nucleophilic attack of the substrate’s carbonyl carbon atom leading to the formation of a covalent acyl-enzyme intermediate via tetrahedral transition states sometimes known as the “tetrahedral intermediates.” Simultaneously, a proton is transferred from the serine to the histidine. The resulting tetrahydral intermediate, negatively charged carbonyl oxygen atom (“oxyanion”) is stabilized through interactions with two main chain NH groups in the “oxyanion hole”, while the positively charged histidine is stabilized by a hydrogen bond to the catalytic acid. In the next step, the formed alcohol is released from the substrate and the acid part forms an ester bond with the serine oxygen. This bond, in turn, is hydrolyzed in a two- step mechanism involving a water molecule, and the enzyme is returned to the starting point <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The serine genral base is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called “nucleophilic elbow”, which has become the fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. The histidine acting as general acid-base catalyst is also conserved <cite>Schubot2001 Prates2001</cite>, while the general acid commonly is observed as both a aspartic or glutamic acid <cite>Holck2019</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
<br />
#Lombard2014 pmid=24270786<br />
<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
#Prates2001 pmid=11738044<br />
#Schubot2001 pmid=11601976<br />
<br />
#Holck2019 pmid=31558605<br />
<br />
</biblio><br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=14293User:Casper Wilkens2019-09-30T13:52:27Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third post at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
<br />
#Holck2019b pmid=31558605<br />
<br />
#Pilgaard2019a pmid=31451726<br />
<br />
#Holck2019a pmid=31307573<br />
#Wilkens2019a pmid=30315603<br />
#Wilkens2018a pmid=30483298<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=14292User:Casper Wilkens2019-09-30T13:51:43Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third post at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
<br />
#Holck2019b pmid=31558605<br />
<br />
#Pilgaard2019a pmid=31451726<br />
<br />
#Wilkens2019b pmid=31307573<br />
#Wilkens2019a pmid=30315603<br />
#Wilkens2018a pmid=30483298<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=14234User:Casper Wilkens2019-08-29T06:26:46Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third post at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Pilgaard2019a pmid=31451726<br />
#Wilkens2019b pmid=31307573<br />
#Wilkens2019a pmid=30315603<br />
#Wilkens2018a pmid=30483298<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=14040User:Casper Wilkens2019-07-21T09:57:47Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third post at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
<br />
#Wilkens2019b pmid=31307573<br />
<br />
#Wilkens2019a pmid=30315603<br />
#Wilkens2018a pmid=30483298<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=14039User:Casper Wilkens2019-07-21T09:57:07Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third post at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
<br />
#Wilkens2019b pmid=31307573<br />
<br />
#Wilkens2018a pmid=30315603<br />
#Wilkens2018b pmid=30483298<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13833Carbohydrate Esterase Family 12019-06-25T12:13:55Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, the general mechanism of hydrolysis, involving the serine nucleophile, an activating histidine, and a catalytic acid, appears to be conserved. After substrate binding, the serine is activated by the histidine, which allows the nucleophilic attack of the substrate’s carbonyl carbon atom leading to the formation of a covalent acyl-enzyme intermediate via tetrahedral transition states sometimes known as the “tetrahedral intermediates.” Simultaneously, a proton is transferred from the serine to the histidine. The resulting tetrahydral intermediate, negatively charged carbonyl oxygen atom (“oxyanion”) is stabilized through interactions with two main chain NH groups in the “oxyanion hole”, while the positively charged histidine is stabilized by a hydrogen bond to the catalytic acid. In the next step, the formed alcohol is released from the substrate and the acid part forms an ester bond with the serine oxygen. This bond, in turn, is hydrolyzed in a two- step mechanism involving a water molecule, and the enzyme is returned to the starting point <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The serine nucleophile is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called “nucleophilic elbow”, which has become the fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>.<br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
<br />
#Prates2001 pmid=11738044<br />
<br />
#Schubot2001 pmid=11601976<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13832Carbohydrate Esterase Family 12019-06-25T12:07:06Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, the general mechanism of hydrolysis, involving the serine nucleophile, an activating histidine, and a catalytic acid, appears to be conserved. After substrate binding, the serine is activated by the histidine, which allows the nucleophilic attack of the substrate’s carbonyl carbon atom leading to the formation of a covalent acyl-enzyme intermediate via tetrahedral transition states sometimes known as the “tetrahedral intermediates.” Simultaneously, a proton is transferred from the serine to the histidine. The resulting tetrahydral intermediate, negatively charged carbonyl oxygen atom (“oxyanion”) is stabilized through interactions with two main chain NH groups in the “oxyanion hole”, while the positively charged histidine is stabilized by a hydrogen bond to the catalytic acid. In the next step, the formed alcohol is released from the substrate and the acid part forms an ester bond with the serine oxygen. This bond, in turn, is hydrolyzed in a two- step mechanism involving a water molecule, and the enzyme is returned to the starting point <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
The serine nucleophile is located at the center of a universally conserved pentapeptide with the consensus sequence G-X-S-X-G. This pentapeptide segment constitutes the so-called “nucleophilic elbow”, which has become the fingerprint feature commonly used to identify proteins of this enzyme family based on their primary structure alone <cite>Schubot2001</cite>. <br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. The crystal structure of 9 CE1s have been determined - 4 mycosyltransferases, 4 ferulic acid esterases and 1 acetyl xylan esterase <cite>Lombard2014</cite>. <br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
<br />
#Prates2001 pmid=11738044<br />
<br />
#Schubot2001 pmid=11601976<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13831Carbohydrate Esterase Family 12019-06-25T12:05:30Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
CE1 enzymes target a large variety of substrates, however, the general mechanism of hydrolysis, involving the serine nucleophile, an activating histidine, and a catalytic acid, appears to be conserved. After substrate binding, the serine is activated by the histidine, which allows the nucleophilic attack of the substrate’s carbonyl carbon atom leading to the formation of a covalent acyl-enzyme intermediate via tetrahedral transition states sometimes known as the “tetrahedral intermediates.” Simultaneously, a proton is transferred from the serine to the histidine. The resulting tetrahydral intermediate, negatively charged carbonyl oxygen atom (“oxyanion”) is stabilized through interactions with two main chain NH groups in the “oxyanion hole”, while the positively charged histidine is stabilized by a hydrogen bond to the catalytic acid. In the next step, the formed alcohol is released from the substrate and the acid part forms an ester bond with the serine oxygen. This bond, in turn, is hydrolyzed in a two- step mechanism involving a water molecule, and the enzyme is returned to the starting point <cite>Schubot2001 Prates2001</cite>. <br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. The crystal structure of 9 CE1s have been determined - 4 mycosyltransferases, 4 ferulic acid esterases and 1 acetyl xylan esterase <cite>Lombard2014</cite>. <br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
<br />
#Prates2001 pmid=11738044<br />
<br />
#Schubot2001 pmid=11601976<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_62&diff=13703Glycoside Hydrolase Family 622019-05-22T08:36:28Z<p>Casper Wilkens: </p>
<hr />
<div>{{CuratorApproved}}<br />
* [[Author]]: [[User:Harry Gilbert|Harry Gilbert]] and ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: [[User:Harry Gilbert|Harry Gilbert]]<br />
----<br />
<br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH62'''<br />
|-<br />
|'''Clan''' <br />
|GH-F<br />
|-<br />
|'''Mechanism'''<br />
| inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH62.html<br />
|}<br />
</div><br />
<br />
== Substrate specificities ==<br />
This small family of [[glycoside hydrolases]] comprises both eukaryotic and prokaryotic enzymes. All the characterized enzymes in this family are arabinofuranosidases and the majority act on xylose moieties in xylan and arabinose moieties in arabinan that are single substituted with &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains <cite>Wilkens2017</cite> with ''K''<sub>cat</sub> ranging from 0.3 to 180 s<sup>-1</sup> on wheat arabinoxylan <cite>Maehara2014 Wang2014 Wilkens2016</cite>. Interestlingly, the preference for &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains varies for GH62s, hence the catalytic rate for the two side chains vary<cite>Wilkens016 Sarch2019</cite>. However, a single GH62 enzyme from ''Pencillium oxalicum'' exclusively act on the &alpha;-1,3-L-arabinofuranose side chains <cite>Hu2018</cite>. The GH62 enzymes also display limited non-specific arabinofuranosidase activity; for example the arabinofuranosidases exhibit no <cite>Kellett1990</cite> or very little <cite>Maehara2014 Wang2014</cite> activity against 4-nitrophenyl &alpha;-L-arabinofuranoside. Several of these enzymes contain carbohydrate binding modules that target cellulose<cite>Kellett1990</cite> or xylan<cite>Dupont1998</cite>.<br />
== Kinetics and Mechanism ==<br />
The stereochemical course of arabinose was followed by <sup>1</sup>H NMR during hydrolysis of a 50:50 mixture of XA<sup>2</sup>XX:XA<sup>3</sup>XX by ''Aspergillus nidulans'' &alpha;-L-arabinofuranosidase A, resulting in the release of &beta;-furanose demonstrating that GH62 enzymes in fact are [[inverting]] enzymes <cite>Wilkens2016</cite>, which is in accordance with the known inverting mechanism for [[GH43]] <cite>Pitson1996</cite> constituting [[clan]] F with GH62 <cite>Lombard2014</cite>. Due to arabinose's fast mutarotation, however, the anomeric signal decreased considerably already after 1 min, which was overcome by recording the first spectrum 23 s after enzyme addition <cite>Wilkens2016</cite>.<br />
<br />
== Catalytic Residues ==<br />
Asp ([[general acid]]) and Glu ([[general base]]), as suggested by tertiary structures <cite>Maehara2014 Siguier2014 Wang2014</cite> and supported by site-directed mutagenesis and kinetic data <cite>Maehara2014 Wang2014</cite>.<br />
<br />
== Three-dimensional structures ==<br />
Based on its location in [[clan]] F together with [[GH43]], enzymes from family GH62s were predicted to display a 5-fold &beta;-propeller fold. This hypothesis was confirmed by three papers published in 2014 <cite>Maehara2014 Siguier2014 Wang2014</cite>. The predicted catalytic general acid, catalytic general base and pKa modulator <cite>Vincent1997</cite> were also confirmed by mutagenesis data <cite>Maehara2014 Wang2014</cite>. The active site arabinose-containing pocket opens up into a cleft or channel that binds the xylooligosaccharides and thus the xylan chain. The residues that interact with the substrate backbone were identified for ''Streptomyces coelicolor'' &alpha;-L-arabinofuranosidase A (ScAbf62A) in a crystal structure in complex with xylopentaose, which spanned subsite +2R to +4NR <cite>Maehara2014</cite>. In this respect a conserved tyrosine, present on a mobile loop, was shown to make an important contribution to substrate binding through hydrophobic interactions with the arabinose located in the active site <cite>Contesini2017</cite>. Remarkably, the xylan main chain bound in two orientations in the crystal structures of ScAbf62A and ''Streptomyces thermoviolaceus'' &alpha;-L-arabinofuranosidase A, as may be required to position both single &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains in subsite -1 for productive binding in the active site pocket <cite>Maehara2014 Wang2014</cite>. The preference for either &alpha;-1,2 or &alpha;-1,3-L-arabinofuranose side chains seems to correlate with the presence of an arginine residue interacting with the xylan main chain at the +2R subsite <cite>Sarch2019</cite>.<br />
<br />
== Family Firsts ==<br />
;First sterochemistry determination: Determined for ''Aspergillus nidulans'' &alpha;-L-arabinofuranosidase A by <sup>1</sup>H NMR <cite>Wilkens2016</cite>.<br />
;First [[general acid]] residue identification: 3D structural data <cite>Maehara2014 Siguier2014 Wang2014</cite> in concert with supporting mutagenesis data <cite>Maehara2014 Wang2014</cite>. <br />
;First [[general base]] residue identification: 3D structural data <cite>Maehara2014 Siguier2014 Wang2014</cite> in concert with supporting mutagenesis data <cite>Maehara2014 Wang2014</cite>.<br />
;First 3-D structure: Several papers in 2014 reveal the 5-fold &beta;-propeller fold <cite>Maehara2014 Siguier2014 Wang2014</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Kellett1990 pmid=2125205<br />
#Pons2004 pmid=14747991<br />
#Dupont1998 pmid=9461488<br />
#Vincent1997 pmid=9148759<br />
#Maehara2014 pmid=24482228<br />
#Siguier2014 pmid=24394409<br />
#Wang2014 pmid=24951792<br />
#Contesini2017 pmid=28890404<br />
#Wilkens2017 pmid=28669588<br />
#Wilkens2016 pmid=26946172<br />
#Hu2018 pmid=29611040<br />
#Pitson1996 pmid=8946944<br />
#Lombard2014 pmid=24270786<br />
<br />
#Sarch2019 pmid=30936018<br />
</biblio><br />
<!-- DO NOT REMOVE THIS CATEGORY TAG! (...but please delete the nowiki tags before saving.)--><br />
[[Category:Glycoside Hydrolase Families|GH062]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_62&diff=13702Glycoside Hydrolase Family 622019-05-22T08:35:53Z<p>Casper Wilkens: </p>
<hr />
<div>{{CuratorApproved}}<br />
* [[Author]]: [[User:Harry Gilbert|Harry Gilbert]] and ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: [[User:Harry Gilbert|Harry Gilbert]]<br />
----<br />
<br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH62'''<br />
|-<br />
|'''Clan''' <br />
|GH-F<br />
|-<br />
|'''Mechanism'''<br />
| inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH62.html<br />
|}<br />
</div><br />
<br />
== Substrate specificities ==<br />
This small family of [[glycoside hydrolases]] comprises both eukaryotic and prokaryotic enzymes. All the characterized enzymes in this family are arabinofuranosidases and the majority act on xylose moieties in xylan and arabinose moieties in arabinan that are single substituted with &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains <cite>Wilkens2017</cite> with ''K''<sub>cat</sub> ranging from 0.3 to 180 s<sup>-1</sup> on wheat arabinoxylan <cite>Maehara2014 Wang2014 Wilkens2016</cite>. Interestlingly, the preference for &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains varies for GH62s, hence the catalytic rate for the two side chains vary<cite>Wilkens016 Sarch2019</cite>. However, a single GH62 enzyme from ''Pencillium oxalicum'' exclusively act on the &alpha;-1,3-L-arabinofuranose side chains <cite>Hu2018</cite>. The GH62 enzymes also display limited non-specific arabinofuranosidase activity; for example the arabinofuranosidases exhibit no <cite>Kellett1990</cite> or very little <cite>Maehara2014 Wang2014</cite> activity against 4-nitrophenyl &alpha;-L-arabinofuranoside. Several of these enzymes contain carbohydrate binding modules that target cellulose<cite>Kellett1990</cite> or xylan<cite>Dupont1998</cite>.<br />
== Kinetics and Mechanism ==<br />
The stereochemical course of arabinose was followed by <sup>1</sup>H NMR during hydrolysis of a 50:50 mixture of XA<sup>2</sup>XX:XA<sup>3</sup>XX by ''Aspergillus nidulans'' &alpha;-L-arabinofuranosidase A, resulting in the release of &beta;-furanose demonstrating that GH62 enzymes in fact are [[inverting]] enzymes <cite>Wilkens2016</cite>, which is in accordance with the known inverting mechanism for [[GH43]] <cite>Pitson1996</cite> constituting [[clan]] F with GH62 <cite>Lombard2014</cite>. Due to arabinose's fast mutarotation, however, the anomeric signal decreased considerably already after 1 min, which was overcome by recording the first spectrum 23 s after enzyme addition <cite>Wilkens2016</cite>.<br />
<br />
== Catalytic Residues ==<br />
Asp ([[general acid]]) and Glu ([[general base]]), as suggested by tertiary structures <cite>Maehara2014 Siguier2014 Wang2014</cite> and supported by site-directed mutagenesis and kinetic data <cite>Maehara2014 Wang2014</cite>.<br />
<br />
== Three-dimensional structures ==<br />
Based on its location in [[clan]] F together with [[GH43]], enzymes from family GH62s were predicted to display a 5-fold &beta;-propeller fold. This hypothesis was confirmed by three papers published in 2014 <cite>Maehara2014 Siguier2014 Wang2014</cite>. The predicted catalytic general acid, catalytic general base and pKa modulator <cite>Vincent1997</cite> were also confirmed by mutagenesis data <cite>Maehara2014 Wang2014</cite>. The active site arabinose-containing pocket opens up into a cleft or channel that binds the xylooligosaccharides and thus the xylan chain. The residues that interact with the substrate backbone were identified for ''Streptomyces coelicolor'' &alpha;-L-arabinofuranosidase A (ScAbf62A) in a crystal structure in complex with xylopentaose, which spanned subsite +2R to +4NR <cite>Maehara2014</cite>. In this respect a conserved tyrosine, present on a mobile loop, was shown to make an important contribution to substrate binding through hydrophobic interactions with the arabinose located in the active site <cite>Contesini2017</cite>. Remarkably, the xylan main chain bound in two orientations in the crystal structures of ScAbf62A and ''Streptomyces thermoviolaceus'' &alpha;-L-arabinofuranosidase A, as may be required to position both single &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains in subsite -1 for productive binding in the active site pocket <cite>Maehara2014 Wang2014</cite>. The preference for either &alpha;-1,2 or &alpha;-1,3-L-arabinofuranose side chains seems to correlate with the presence of an arginine residue interacting with the xylan manin chain at the +2R subsite <cite>Sarch2019</cite>.<br />
<br />
== Family Firsts ==<br />
;First sterochemistry determination: Determined for ''Aspergillus nidulans'' &alpha;-L-arabinofuranosidase A by <sup>1</sup>H NMR <cite>Wilkens2016</cite>.<br />
;First [[general acid]] residue identification: 3D structural data <cite>Maehara2014 Siguier2014 Wang2014</cite> in concert with supporting mutagenesis data <cite>Maehara2014 Wang2014</cite>. <br />
;First [[general base]] residue identification: 3D structural data <cite>Maehara2014 Siguier2014 Wang2014</cite> in concert with supporting mutagenesis data <cite>Maehara2014 Wang2014</cite>.<br />
;First 3-D structure: Several papers in 2014 reveal the 5-fold &beta;-propeller fold <cite>Maehara2014 Siguier2014 Wang2014</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Kellett1990 pmid=2125205<br />
#Pons2004 pmid=14747991<br />
#Dupont1998 pmid=9461488<br />
#Vincent1997 pmid=9148759<br />
#Maehara2014 pmid=24482228<br />
#Siguier2014 pmid=24394409<br />
#Wang2014 pmid=24951792<br />
#Contesini2017 pmid=28890404<br />
#Wilkens2017 pmid=28669588<br />
#Wilkens2016 pmid=26946172<br />
#Hu2018 pmid=29611040<br />
#Pitson1996 pmid=8946944<br />
#Lombard2014 pmid=24270786<br />
<br />
#Sarch2019 pmid=30936018<br />
</biblio><br />
<!-- DO NOT REMOVE THIS CATEGORY TAG! (...but please delete the nowiki tags before saving.)--><br />
[[Category:Glycoside Hydrolase Families|GH062]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_62&diff=13701Glycoside Hydrolase Family 622019-05-22T08:34:28Z<p>Casper Wilkens: </p>
<hr />
<div>{{CuratorApproved}}<br />
* [[Author]]: [[User:Harry Gilbert|Harry Gilbert]] and ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: [[User:Harry Gilbert|Harry Gilbert]]<br />
----<br />
<br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH62'''<br />
|-<br />
|'''Clan''' <br />
|GH-F<br />
|-<br />
|'''Mechanism'''<br />
| inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH62.html<br />
|}<br />
</div><br />
<br />
== Substrate specificities ==<br />
This small family of [[glycoside hydrolases]] comprises both eukaryotic and prokaryotic enzymes. All the characterized enzymes in this family are arabinofuranosidases and the majority act on xylose moieties in xylan and arabinose moieties in arabinan that are single substituted with &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains <cite>Wilkens2017</cite> with ''K''<sub>cat</sub> ranging from 0.3 to 180 s<sup>-1</sup> on wheat arabinoxylan <cite>Maehara2014 Wang2014 Wilkens2016</cite>. Interestlingly, the preference for &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains varies for GH62s <cite>Wilkens016 Sarch2019</cite>. However, a single GH62 enzyme from ''Pencillium oxalicum'' exclusively act on the &alpha;-1,3-L-arabinofuranose side chains <cite>Hu2018</cite>. The GH62 enzymes also display limited non-specific arabinofuranosidase activity; for example the arabinofuranosidases exhibit no <cite>Kellett1990</cite> or very little <cite>Maehara2014 Wang2014</cite> activity against 4-nitrophenyl &alpha;-L-arabinofuranoside. Several of these enzymes contain carbohydrate binding modules that target cellulose<cite>Kellett1990</cite> or xylan<cite>Dupont1998</cite>.<br />
== Kinetics and Mechanism ==<br />
The stereochemical course of arabinose was followed by <sup>1</sup>H NMR during hydrolysis of a 50:50 mixture of XA<sup>2</sup>XX:XA<sup>3</sup>XX by ''Aspergillus nidulans'' &alpha;-L-arabinofuranosidase A, resulting in the release of &beta;-furanose demonstrating that GH62 enzymes in fact are [[inverting]] enzymes <cite>Wilkens2016</cite>, which is in accordance with the known inverting mechanism for [[GH43]] <cite>Pitson1996</cite> constituting [[clan]] F with GH62 <cite>Lombard2014</cite>. Due to arabinose's fast mutarotation, however, the anomeric signal decreased considerably already after 1 min, which was overcome by recording the first spectrum 23 s after enzyme addition <cite>Wilkens2016</cite>.<br />
<br />
== Catalytic Residues ==<br />
Asp ([[general acid]]) and Glu ([[general base]]), as suggested by tertiary structures <cite>Maehara2014 Siguier2014 Wang2014</cite> and supported by site-directed mutagenesis and kinetic data <cite>Maehara2014 Wang2014</cite>.<br />
<br />
== Three-dimensional structures ==<br />
Based on its location in [[clan]] F together with [[GH43]], enzymes from family GH62s were predicted to display a 5-fold &beta;-propeller fold. This hypothesis was confirmed by three papers published in 2014 <cite>Maehara2014 Siguier2014 Wang2014</cite>. The predicted catalytic general acid, catalytic general base and pKa modulator <cite>Vincent1997</cite> were also confirmed by mutagenesis data <cite>Maehara2014 Wang2014</cite>. The active site arabinose-containing pocket opens up into a cleft or channel that binds the xylooligosaccharides and thus the xylan chain. The residues that interact with the substrate backbone were identified for ''Streptomyces coelicolor'' &alpha;-L-arabinofuranosidase A (ScAbf62A) in a crystal structure in complex with xylopentaose, which spanned subsite +2R to +4NR <cite>Maehara2014</cite>. In this respect a conserved tyrosine, present on a mobile loop, was shown to make an important contribution to substrate binding through hydrophobic interactions with the arabinose located in the active site <cite>Contesini2017</cite>. Remarkably, the xylan main chain bound in two orientations in the crystal structures of ScAbf62A and ''Streptomyces thermoviolaceus'' &alpha;-L-arabinofuranosidase A, as may be required to position both single &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains in subsite -1 for productive binding in the active site pocket <cite>Maehara2014 Wang2014</cite>. The preference for either &alpha;-1,2 or &alpha;-1,3-L-arabinofuranose side chains seems to correlate with the presence of an arginine residue interacting with the xylan manin chain at the +2R subsite <cite>Sarch2019</cite>.<br />
<br />
== Family Firsts ==<br />
;First sterochemistry determination: Determined for ''Aspergillus nidulans'' &alpha;-L-arabinofuranosidase A by <sup>1</sup>H NMR <cite>Wilkens2016</cite>.<br />
;First [[general acid]] residue identification: 3D structural data <cite>Maehara2014 Siguier2014 Wang2014</cite> in concert with supporting mutagenesis data <cite>Maehara2014 Wang2014</cite>. <br />
;First [[general base]] residue identification: 3D structural data <cite>Maehara2014 Siguier2014 Wang2014</cite> in concert with supporting mutagenesis data <cite>Maehara2014 Wang2014</cite>.<br />
;First 3-D structure: Several papers in 2014 reveal the 5-fold &beta;-propeller fold <cite>Maehara2014 Siguier2014 Wang2014</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Kellett1990 pmid=2125205<br />
#Pons2004 pmid=14747991<br />
#Dupont1998 pmid=9461488<br />
#Vincent1997 pmid=9148759<br />
#Maehara2014 pmid=24482228<br />
#Siguier2014 pmid=24394409<br />
#Wang2014 pmid=24951792<br />
#Contesini2017 pmid=28890404<br />
#Wilkens2017 pmid=28669588<br />
#Wilkens2016 pmid=26946172<br />
#Hu2018 pmid=29611040<br />
#Pitson1996 pmid=8946944<br />
#Lombard2014 pmid=24270786<br />
<br />
#Sarch2019 pmid=30936018<br />
</biblio><br />
<!-- DO NOT REMOVE THIS CATEGORY TAG! (...but please delete the nowiki tags before saving.)--><br />
[[Category:Glycoside Hydrolase Families|GH062]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13507Carbohydrate Esterase Family 12019-02-04T11:20:31Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
Mycolyltransferases transfer of the mycolyl group from α,α′-trehalose monomycolate to a second α,α′-trehalose monomycolate molecule forming α,α′-trehalose dimycolate <cite>Belisle1997</cite><br />
Ferulic acid esterases hydrolyze the ester bond linking the ferulic acid to the arabinose moiety, which decorate certain types of xylan. <br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. The crystal structure of 9 CE1s have been determined - 4 mycosyltransferases, 4 ferulic acid esterases and 1 acetyl xylan esterase <cite>Lombard2014</cite>. <br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13506Carbohydrate Esterase Family 12019-02-04T11:14:51Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC [{{EClink}}3.1.1.72 3.1.1.72]), feruloyl esterases (EC [{{EClink}}3.1.1.73 3.1.1.73]), cinnamoyl esterases (EC 3.1.1.-), carboxylesterases (EC [{{EClink}}3.1.1.1 3.1.1.1]), S-formylglutathione hydrolases (EC [{{EClink}}3.1.2.12 3.1.2.12]), diacylglycerol ''O''-acyltransferases (EC [{{EClink}}2.3.1.20 2.3.1.20]), and thehalose 6-''O''-mycolyltransferases (EC [{{EClink}}2.3.1.122 2.3.1.122]) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
Mycolyltransferases transfer of the mycolyl group from α,α′-trehalose monomycolate to a second α,α′-trehalose monomycolate molecule forming α,α′-trehalose dimycolate <cite>Belisle1997</cite><br />
Ferulic acid esterases hydrolyze the ester bond linking the ferulic acid to the arabinose moiety, which decorate certain types of xylan. <br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of a central β-sheet with 8 or 9 strands connected by α-helices <cite>Ollis1992</cite>. <br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13503Carbohydrate Esterase Family 12019-02-01T14:01:44Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol ''O''-acyltransferases (EC 2.3.1.20), and thehalose 6-''O''-mycolyltransferases (EC 2.3.1.122) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
Mycolyltransferases transfer of the mycolyl group from α,α′-trehalose monomycolate to a second α,α′-trehalose monomycolate molecule forming α,α′-trehalose dimycolate <cite>Belisle1997</cite><br />
Ferulic acid esterases hydrolyze the ester bond linking the ferulic acid to the arabinose moiety, which decorate certain types of xylan. <br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of central β-strands connected by α-helices <cite>Ollis1992</cite>. <br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13502Carbohydrate Esterase Family 12019-02-01T13:54:40Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol ''O''-acyltransferases (EC 2.3.1.20), and thehalose 6-''O''-mycolyltransferases (EC 2.3.1.122) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
Mycolyltransferases transfer of the mycolyl group from α,α′-trehalose monomycolate to a second α,α′-trehalose monomycolate molecule forming α,α′-trehalose dimycolate <cite>Belisle1997</cite><br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of central β-strands connected by α-helices <cite>Ollis1992</cite>. <br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
#Belisle1997 pmid=9162010<br />
#Ollis1992 pmid=1409539<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13501Carbohydrate Esterase Family 12019-02-01T13:23:39Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol ''O''-acyltransferases (EC 2.3.1.20), and thehalose 6-''O''-mycolyltransferases (EC 2.3.1.122) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of central β-strands connected by α-helices <cite>Ollis1992</cite>. <br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism, which involved the highly conserved catalytic Ser-Glu-His triad <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
<br />
#Ollis1992 pmid1409539<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13500Carbohydrate Esterase Family 12019-02-01T13:22:27Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol ''O''-acyltransferases (EC 2.3.1.20), and thehalose 6-''O''-mycolyltransferases (EC 2.3.1.122) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of central β-strands connected by α-helices <cite>Ollis1992</cite>. <br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism <cite>Ronning2000</cite>.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
<br />
#Ollis1992 pmid1409539<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13499Carbohydrate Esterase Family 12019-02-01T13:22:05Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol ''O''-acyltransferases (EC 2.3.1.20), and thehalose 6-''O''-mycolyltransferases (EC 2.3.1.122) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of central β-strands connected by α-helices <cite>Ollis1992</cite>. <br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: The crystal structure of ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in complex with the covalently bound inhibitor, diethyl phosphate gave the first insight into the mechanism.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
<br />
#Ollis1992 pmid1409539<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13498Carbohydrate Esterase Family 12019-02-01T13:10:46Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol ''O''-acyltransferases (EC 2.3.1.20), and thehalose 6-''O''-mycolyltransferases (EC 2.3.1.122) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
CE1's are members of the α/β-hydrolase superfamily <cite>Ronning2000</cite>, which are comprised of central β-strands connected by α-helices <cite>Ollis1992</cite>. <br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: Content is to be added here.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
#Ronning2000 pmid=10655617<br />
<br />
#Ollis1992 pmid1409539<br />
<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13497Carbohydrate Esterase Family 12019-02-01T12:51:26Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol ''O''-acyltransferases (EC 2.3.1.20), and thehalose 6-''O''-mycolyltransferases (EC 2.3.1.122) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First characterized: Content is to be added here.<br />
;First mechanistic insight: Content is to be added here.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
<br />
#Ronning2000 pmid=10655617<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13496Carbohydrate Esterase Family 12019-02-01T12:44:37Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol ''O''-acyltransferases (EC 2.3.1.20), and thehalose 6-''O''-mycolyltransferases (EC 2.3.1.122) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase crystal structure in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
<br />
#Ronning2000 pmid=10655617<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Carbohydrate_Esterase_Family_1&diff=13495Carbohydrate Esterase Family 12019-02-01T12:42:46Z<p>Casper Wilkens: </p>
<hr />
<div><!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --><br />
{{UnderConstruction}}<br />
* [[Author]]: ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: <br />
----<br />
<br />
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family --><br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Carbohydrate Esterase Family 1'''<br />
|-<br />
|'''Clan''' <br />
|GH-x<br />
|-<br />
|'''Mechanism'''<br />
|retaining/inverting<br />
|-<br />
|'''Active site residues'''<br />
|known/not known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}CE1.html<br />
|}<br />
</div><br />
<!-- This is the end of the table --><br />
<br />
<br />
== Substrate specificities ==<br />
Carbohydrate esterase family 1 (CE1) is one of the biggest and most diverse CE families including acetylxylan esterases (EC 3.1.1.72), feruloyl esterases (EC 3.1.1.73), cinnamoyl esterases (EC 3.1.1-), carboxylesterases (EC 3.1.1.1), S-formylglutathione hydrolases (EC 3.1.2.12), diacylglycerol ''O''-acyltransferases (EC 2.3.1.20), and thehalose 6-''O''-mycolyltransferases (EC 2.3.1.122) and others <cite>Lombard2014</cite>.<br />
<br />
<br />
<br />
== Kinetics and Mechanism ==<br />
Content is to be added here.<br />
<br />
== Catalytic Residues ==<br />
Content is to be added here.<br />
<br />
== Three-dimensional structures ==<br />
Content is to be added here.<br />
<br />
== Family Firsts ==<br />
;First stereochemistry determination: Content is to be added here.<br />
;First catalytic nucleophile identification: Content is to be added here.<br />
;First general acid/base residue identification: Content is to be added here.<br />
;First 3-D structure: ''Mycobacterium'' ''tuberculosis'' H37Rv mycolyltransferase in 2000 <cite>Ronning2000</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Lombard2014 pmid=24270786<br />
<br />
#Ronning2000 pmid=10655617<br />
</biblio><br />
<br />
[[Category:Carbohydrate Esterase Families|CE001]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=13471User:Casper Wilkens2019-01-02T13:52:37Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third post at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
<br />
#Wilkens2018a pmid=30315603<br />
<br />
#Wilkens2018b pmid=30483298<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=13470User:Casper Wilkens2019-01-02T13:49:50Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third post at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
<br />
#Wilkens2018b pmid=30483298<br />
<br />
#Wilkens2018a pmid=30315603<br />
<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=User:Casper_Wilkens&diff=13387User:Casper Wilkens2018-10-21T16:53:25Z<p>Casper Wilkens: </p>
<hr />
<div>[[Image:Blank_user-200px.png|200px|right]]<br />
Casper Wilkens obtained his B.Sc. in Molecular Biology and Chemistry from Roskilde University under the supervision of Peter Westh and others, M.Sc. in Biochemistry from University of Copenhagen under the supervision of ^^^Leila Lo Leggio^^^, completed his PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem in 2014 at the Department of Systems Biology, Technical University of Denmark. During his PhD Casper studied [[Surface Binding Site]]s and continued to do so during his first Post Doc at the same place. After a short Post Doc at Aalborg Univeristy Casper returned to the Technical University of Denmark and completed his third post at the Department of Chemical and Biochemical Engineering with Lene Lange and Anne S. Meyer. In 2018 Casper was appointed Assistant Professor at [http://www.bioengineering.dtu.dk/ Department of Biotechnology and Biomedicine] at the Technical University of Denmark. Casper's research interests concern discovery of novel carbohydrate-active enzymes and their structure-function relationships. <br />
<br />
<br />
----<br />
<br />
<biblio><br />
#Wilkens2018a pmid=30315603<br />
#CAZypediaConsortium2018 pmid=29040563<br />
#Wilkens2017b pmid=28649277<br />
#Wilkens2017a pmid=28669588<br />
#Rydahl2017 pmid=28839196<br />
#Cockburn2017 pmid=28417364<br />
#Cockburn2016 pmid=27504624<br />
#Wilkens2016b pmid=26946172<br />
#Wilkens2016a pmid=26763114<br />
#Wilkens2015 Wilkens, C., Cockburn, D., Andersen, S., Petersen, B. O., Ruzanski, C., Field, R. A., Hindsgaul, O., Nakai, H., McCleary, B., Smith, A. M., Abou Hachem, M. and Svensson, B. (2015) Analysis of surface binding sites (SBS) within GH62, GH13 and GH77 . J. Appl. Glycosci., 62, 87-93. [https://doi.org/10.5458/jag.jag.JAG-2015_006 DOI: 10.5458/jag.jag.JAG-2015_006]<br />
#Wilkens2014b Wilkens, C., Cuesta-Seijo, J. A., Palcic, M. and Svensson, B. (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I . Biologia, 69, 1118-1121. [https://doi.org/10.2478/s11756-014-0418-0 DOI: 10.2478/s11756-014-0418-0]<br />
#Cockburn2014 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A.M., Field, R.A., Willemoës, M., Abou Hachem, M., and Svensson B. (2014) Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia, 69, 705-712. [http://dx.doi.org/10.2478/s11756-014-0373-9 DOI: 10.2478/s11756-014-0373-9]<br />
<br />
#Wilkens2014a pmid=25025819<br />
<br />
#Moller2013 Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës M., and B. Svensson (2013) ''Surface Binding Sites (SBS), Mechanism and Regulation of 2 Enzymes Degrading Amylopectin and α-limit Dextrins.'' J. Appl. Glycosci. EPub March 21. [http://dx.doi.org/10.5458/jag.jag.JAG-2012_023 DOI: 10.5458/jag.jag.JAG-2012_023]<br />
<br />
#Kristiansen2012 pmid=23000739<br />
<br />
#Wilkens2008 pmid=19137192<br />
</biblio><br />
<!-- Do not remove this Category tag --><br />
[[Category:Contributors|Wilkens,Casper]]</div>Casper Wilkenshttps://www.cazypedia.org/index.php?title=Glycoside_Hydrolase_Family_62&diff=13367Glycoside Hydrolase Family 622018-09-27T07:44:00Z<p>Casper Wilkens: </p>
<hr />
<div>{{CuratorApproved}}<br />
* [[Author]]: [[User:Harry Gilbert|Harry Gilbert]] and ^^^Casper Wilkens^^^<br />
* [[Responsible Curator]]: [[User:Harry Gilbert|Harry Gilbert]]<br />
----<br />
<br />
<div style="float:right"><br />
{| {{Prettytable}} <br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH62'''<br />
|-<br />
|'''Clan''' <br />
|GH-F<br />
|-<br />
|'''Mechanism'''<br />
| inverting<br />
|-<br />
|'''Active site residues'''<br />
|Known<br />
|-<br />
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''<br />
|-<br />
| colspan="2" |{{CAZyDBlink}}GH62.html<br />
|}<br />
</div><br />
<br />
== Substrate specificities ==<br />
This small family of [[glycoside hydrolases]] comprises both eukaryotic and prokaryotic enzymes. All the characterized enzymes in this family are arabinofuranosidases and the majority act on xylose moieties in xylan and arabinose moieties in arabinan that are single substituted with &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains <cite>Wilkens2017</cite> with ''K''<sub>cat</sub> ranging from 0.3 to 180 s<sup>-1</sup> on wheat arabinoxylan <cite>Maehara2014 Wang2014 Wilkens2016</cite>. However, a single GH62 enzyme from ''Pencillium oxalicum'' exclusively act on the &alpha;-1,3-L-arabinofuranose side chains <cite>Hu2018</cite>. The GH62 enzymes also display limited non-specific arabinofuranosidase activity; for example the arabinofuranosidases exhibit no <cite>Kellett1990</cite> or very little <cite>Maehara2014 Wang2014</cite> activity against 4-nitrophenyl &alpha;-L-arabinofuranoside. Several of these enzymes contain carbohydrate binding modules that target cellulose<cite>Kellett1990</cite> or xylan<cite>Dupont1998</cite>.<br />
== Kinetics and Mechanism ==<br />
The stereochemical course of arabinose was followed by <sup>1</sup>H NMR during hydrolysis of a 50:50 mixture of XA<sup>2</sup>XX:XA<sup>3</sup>XX by ''Aspergillus nidulans'' &alpha;-L-arabinofuranosidase A, resulting in the release of &beta;-furanose demonstrating that GH62 enzymes in fact are [[inverting]] enzymes <cite>Wilkens2016</cite>, which is in accordance with the known inverting mechanism for [[GH43]] <cite>Pitson1996</cite> constituting [[clan]] F with GH62 <cite>Lombard2014</cite>. Due to arabinose's fast mutarotation, however, the anomeric signal decreased considerably already after 1 min, which was overcome by recording the first spectrum 23 s after enzyme addition <cite>Wilkens2016</cite>.<br />
<br />
== Catalytic Residues ==<br />
Asp ([[general acid]]) and Glu ([[general base]]), as suggested by tertiary structures <cite>Maehara2014 Siguier2014 Wang2014</cite> and supported by site-directed mutagenesis and kinetic data <cite>Maehara2014 Wang2014</cite>.<br />
<br />
== Three-dimensional structures ==<br />
Based on its location in [[clan]] F together with [[GH43]], enzymes from family GH62s were predicted to display a 5-fold &beta;-propeller fold. This hypothesis was confirmed by three papers published in 2014 <cite>Maehara2014 Siguier2014 Wang2014</cite>. The predicted catalytic general acid, catalytic general base and pKa modulator <cite>Vincent1997</cite> were also confirmed by mutagenesis data <cite>Maehara2014 Wang2014</cite>. The active site arabinose-containing pocket opens up into a cleft or channel that binds the xylooligosaccharides and thus the xylan chain. The residues that interact with the substrate backbone were identified for ''Streptomyces coelicolor'' &alpha;-L-arabinofuranosidase A (ScAbf62A) in a crystal structure in complex with xylopentaose, which spanned subsite +2R to +4NR <cite>Maehara2014</cite>. In this respect a conserved tyrosine, present on a mobile loop, was shown to make an important contribution to substrate binding through hydrophobic interactions with the arabinose located in the active site <cite>Contesini2017</cite>. Remarkably, the xylan main chain bound in two orientations in the crystal structures of ScAbf62A and ''Streptomyces thermoviolaceus'' &alpha;-L-arabinofuranosidase A, as may be required to position both single &alpha;-1,2 and &alpha;-1,3-L-arabinofuranose side chains in subsite -1 for productive binding in the active site pocket <cite>Maehara2014 Wang2014</cite>.<br />
<br />
== Family Firsts ==<br />
;First sterochemistry determination: Determined for ''Aspergillus nidulans'' &alpha;-L-arabinofuranosidase A by <sup>1</sup>H NMR <cite>Wilkens2016</cite>.<br />
;First [[general acid]] residue identification: 3D structural data <cite>Maehara2014 Siguier2014 Wang2014</cite> in concert with supporting mutagenesis data <cite>Maehara2014 Wang2014</cite>. <br />
;First [[general base]] residue identification: 3D structural data <cite>Maehara2014 Siguier2014 Wang2014</cite> in concert with supporting mutagenesis data <cite>Maehara2014 Wang2014</cite>.<br />
;First 3-D structure: Several papers in 2014 reveal the 5-fold &beta;-propeller fold <cite>Maehara2014 Siguier2014 Wang2014</cite>.<br />
<br />
== References ==<br />
<biblio><br />
#Kellett1990 pmid=2125205<br />
#Pons2004 pmid=14747991<br />
#Dupont1998 pmid=9461488<br />
#Vincent1997 pmid=9148759<br />
#Maehara2014 pmid=24482228<br />
#Siguier2014 pmid=24394409<br />
#Wang2014 pmid=24951792<br />
#Contesini2017 pmid=28890404<br />
#Wilkens2017 pmid=28669588<br />
#Wilkens2016 pmid=26946172<br />
#Hu2018 pmid=29611040<br />
#Pitson1996 pmid=8946944<br />
<br />
#Lombard2014 pmid=24270786<br />
</biblio><br />
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[[Category:Glycoside Hydrolase Families|GH062]]</div>Casper Wilkens