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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

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].


  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]
  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. 2013;587(14):2193-8. DOI:10.1016/j.febslet.2013.05.041 | PubMed ID:23711369 [Miyazaki2013]

All Medline abstracts: PubMed