Glycoside Hydrolase Family 131 - Revision history

Harry Brumer: Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

2021-12-18T21:19:08Z

Text replacement - "\^\^\^(.*)\^\^\^" to "$1"

Jean-Guy Berrin at 16:30, 26 June 2013

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Jean-Guy Berrin at 15:17, 26 June 2013

2013-06-26T15:17:50Z

Harry Brumer: /* Substrate specificities */

2012-10-30T17:19:07Z

Substrate specificities

Harry Brumer: /* Kinetics and Mechanism */

2012-10-30T17:17:09Z

Kinetics and Mechanism

Jean-Guy Berrin at 16:25, 25 October 2012

2012-10-25T16:25:56Z

Jean-Guy Berrin at 07:28, 16 October 2012

2012-10-16T07:28:59Z

Jean-Guy Berrin at 07:25, 16 October 2012

2012-10-16T07:25:44Z

Harry Brumer: Created page with " {{UnderConstruct..."

2012-10-16T06:34:13Z

Created page with " {{UnderConstruct..."

New page

{{UnderConstruction}}
* [[Author]]: ^^^Jean-Guy Berrin^^^
* [[Responsible Curator]]: ^^^Jean-Guy Berrin^^^
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<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''Glycoside Hydrolase Family GH131'''
|-
|'''Clan'''
|GH-x
|-
|'''Mechanism'''
|retaining/inverting
|-
|'''Active site residues'''
|known/not known
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}GH131.html
|}
</div>


== Substrate specificities ==
Content is to be added here. In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.

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

== Catalytic Residues ==
Content is to be added here.

== Three-dimensional structures ==
Content is to be added here.

== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
;First catalytic nucleophile identification: Content is to be added here.
;First general acid/base residue identification: Content is to be added here.
;First 3-D structure: Content is to be added here.

== References ==
<biblio>
#Cantarel2009 pmid=18838391
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). [http://dx.doi.org/10.1042/BJ20080382 DOI: 10.1042/BJ20080382]
</biblio>

[[Category:Glycoside Hydrolase Families|GH131]]

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 == Three-dimensional structures ==
-Only one crystal structure of a glycoside hydrolase family 131 protein from ''Coprinopsis cinerea'' is available <cite>Miyazaki2013</cite>. The structure of CcGH131A was found to be composed of a β-jelly roll fold and mainly consisted of two β-sheets, sheet-A and sheet-B.
+Only one crystal structure of a glycoside hydrolase family 131 protein from ''Coprinopsis cinerea'' is available <cite>Miyazaki2013</cite>. The structure of CcGH131A was found to be composed of a β-jelly roll fold.
 == Family Firsts ==

@@ Line 38: / Line 38: @@
 == Three-dimensional structures ==
-Only one crystal structure of a glycoside hydrolase family 131 protein from ''Coprinopsis cinerea'' is available <cite>Miyazaki2013</cite>. The structure of CcGH131A was found to be composed of a β-jelly roll fold and mainly consisted of two β-sheets, sheet-A and sheet-B. Arg96, Glu98, Glu138, and His218 are likely to be catalytically critical residues and it was suggested that the catalytic mechanism of CcGH131A is different from that of typical glycosidases <cite>Miyazaki2013</cite>.
+Only one crystal structure of a glycoside hydrolase family 131 protein from ''Coprinopsis cinerea'' is available <cite>Miyazaki2013</cite>. The structure of CcGH131A was found to be composed of a β-jelly roll fold and mainly consisted of two β-sheets, sheet-A and sheet-B.
 == Family Firsts ==

@@ Line 38: / Line 38: @@
 == Three-dimensional structures ==
-Not known.
+Only one crystal structure of a glycoside hydrolase family 131 protein from ''Coprinopsis cinerea'' is available <cite>Miyazaki2013</cite>. The structure of CcGH131A was found to be composed of a β-jelly roll fold and mainly consisted of two β-sheets, sheet-A and sheet-B. Arg96, Glu98, Glu138, and His218 are likely to be catalytically critical residues and it was suggested that the catalytic mechanism of CcGH131A is different from that of typical glycosidases <cite>Miyazaki2013</cite>.
 == Family Firsts ==
@@ Line 44: / Line 44: @@
 ;First catalytic nucleophile identification: No experimental proof.
 ;First general acid/base residue identification: No experimental proof.
-;First 3-D structure: Not known.
+;First 3-D structure: ''Coprinopsis cinerea'' CcGH131A <cite>Miyazaki2013</cite>.
 == References ==
 <biblio>
 #Lafond2012 pmid=23023747
 </biblio>
 [[Category:Glycoside Hydrolase Families|GH131]]

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 == Substrate specificities ==
-This family of [[glycoside hydrolases]] comprises only enzymes of fungal origin. Several of these enzymes contain cellulose-binding CBMs from family 1. Only one member (gene Pa_3_10940) has been characterized to date from the coprophilic ascomycete ''Podospora anserina'' <cite>Lafond2012</cite>. This first member is a broad specificity β-glucanase with exo-β-1,3/1,6- and endo-β-1,4-glucanase activity <cite>Lafond2012</cite>.
+This family of [[glycoside hydrolases]] comprises only enzymes of fungal origin. Several of these enzymes contain predicted cellulose-binding modules from family [{{CAZyDBlink}}CBM1.html CBM1]. Only one member (gene Pa_3_10940) has been characterized to date from the coprophilic ascomycete ''Podospora anserina'' <cite>Lafond2012</cite>. This first member is a broad specificity β-glucanase with exo-β-1,3/1,6- and endo-β-1,4-glucanase activity <cite>Lafond2012</cite>.
 == Kinetics and Mechanism ==

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 == Kinetics and Mechanism ==
-The ''Podospora anserina'' GH131 beta-glucanase displays activity towards a broad range of β-glucan polysaccharides including laminarin, curdlan, pachyman, lichenan, pustulan and also cellulosic derivatives <cite>Lafond2012</cite>. Analysis of the products released from polysaccharides revealed that this β-glucanase is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan substrates. Hydrolysis of short β-(1,3), β-(1,4) and β-(1,3)/β-(1,4) gluco-oligosaccharides confirmed this striking feature and revealed that the enzyme was performing in an exo-mode on the non-reducing end of gluco-oligosaccharides.
+The ''Podospora anserina'' GH131 beta-glucanase displays activity towards a broad range of β-glucan polysaccharides including laminarin, curdlan, pachyman, lichenan, pustulan and also cellulosic derivatives <cite>Lafond2012</cite>. Analysis of the products released from polysaccharides revealed that this β-glucanase is an exo-acting enzyme on β-(1,3)- and β-(1,6)-linked glucan substrates and an endo-acting enzyme on β-(1,4)-linked glucan substrates. Hydrolysis of short β-(1,3), β-(1,4) and β-(1,3)/β-(1,4) gluco-oligosaccharides confirmed this striking feature and revealed that the enzyme acted in an ''exo''-mode on the non-reducing end of gluco-oligosaccharides.
 == Catalytic Residues ==

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 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
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-* [[Author]]: ^^^Jean-Guy Berrin^^^
+* [[Author]]: [[User:Jean-Guy Berrin|Jean-Guy Berrin]]
-* [[Responsible Curator]]:  ^^^Jean-Guy Berrin^^^
+* [[Responsible Curator]]:  [[User:Jean-Guy Berrin|Jean-Guy Berrin]]
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 |-
 |'''Mechanism'''
-|retaining/inverting
+|not known
 |-
 |'''Active site residues'''
-|known/not known
+|not known
 |-
 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''