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Difference between revisions of "Glycoside Hydrolase Family 131"

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* [[Author]]: ^^^Jean-Guy Berrin^^^
 
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== Substrate specificities ==
 
== 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>. This paper describes the creation of GH131 <cite>Lafond2012</cite>
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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>.
  
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
Content is to be added here.
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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.
  
 
== Catalytic Residues ==
 
== Catalytic Residues ==
Content is to be added here.
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Not known.
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==
Content is to be added here.
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Not known.
  
 
== Family Firsts ==
 
== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
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;First stereochemistry determination: No experimental proof.
;First catalytic nucleophile identification: Content is to be added here.
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;First catalytic nucleophile identification: No experimental proof.
;First general acid/base residue identification: Content is to be added here.
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;First general acid/base residue identification: No experimental proof.
;First 3-D structure: Content is to be added here.
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;First 3-D structure: Not known.
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
 
#Lafond2012 pmid=23023747
 
#Lafond2012 pmid=23023747
#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>
 
</biblio>
  
  
 
[[Category:Glycoside Hydrolase Families|GH131]]
 
[[Category:Glycoside Hydrolase Families|GH131]]

Revision as of 09:25, 25 October 2012

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This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.


Glycoside Hydrolase Family GH131
Clan GH-x
Mechanism not known
Active site residues not known
CAZy DB link
http://www.cazy.org/GH131.html


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 [1]. This first member is a broad specificity β-glucanase with exo-β-1,3/1,6- and endo-β-1,4-glucanase activity [1].

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 [1]. 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.

Catalytic Residues

Not known.

Three-dimensional structures

Not known.

Family Firsts

First stereochemistry determination
No experimental proof.
First catalytic nucleophile identification
No experimental proof.
First general acid/base residue identification
No experimental proof.
First 3-D structure
Not known.

References

  1. Lafond M, Navarro D, Haon M, Couturier M, and Berrin JG. (2012). Characterization of a broad-specificity β-glucanase acting on β-(1,3)-, β-(1,4)-, and β-(1,6)-glucans that defines a new glycoside hydrolase family. Appl Environ Microbiol. 2012;78(24):8540-6. DOI:10.1128/AEM.02572-12 | PubMed ID:23023747 [Lafond2012]