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Glycoside Hydrolase Family 131

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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 predicted cellulose-binding modules from family CBM1. 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 acted in an exo-mode on the non-reducing end of gluco-oligosaccharides.

Catalytic Residues

Not known.

Three-dimensional structures

Only one crystal structure of a glycoside hydrolase family 131 protein from Coprinopsis cinerea is available [2]. The structure of CcGH131A was found to be composed of a β-jelly roll fold.

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
Coprinopsis cinerea CcGH131A [2].

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. 78, 8540-6. DOI:10.1128/AEM.02572-12 | PubMed ID:23023747 | HubMed [Lafond2012]
  2. Miyazaki T, Yoshida M, Tamura M, Tanaka Y, Umezawa K, Nishikawa A, and Tonozuka T. (2013) Crystal structure of the N-terminal domain of a glycoside hydrolase family 131 protein from Coprinopsis cinerea. FEBS Lett. 587, 2193-8. DOI:10.1016/j.febslet.2013.05.041 | PubMed ID:23711369 | HubMed [Miyazaki2013]
All Medline abstracts: PubMed | HubMed