Biology:Glycoside hydrolase family 7

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Short description: Enzyme family


Glycosyl hydrolase family 7
PDB 4ovw EBI.jpg
endoglucanase i complexed with epoxybutyl cellobiose
Identifiers
SymbolGlyco_hydro_7
PfamPF00840
Pfam clanCL0004
InterProIPR001722
SCOP21cel / SCOPe / SUPFAM
CAZyGH7
CDDcd07999

In molecular biology, glycoside hydrolase family 7 is a family of glycoside hydrolases EC 3.2.1., which are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy web site,[4][5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6][7]

Glycoside hydrolase family 7 CAZY GH_7 comprises enzymes with several known activities including endoglucanase (EC 3.2.1.4) and cellobiohydrolase (EC 3.2.1.91). These enzymes were formerly known as cellulase family C.

Exoglucanases and cellobiohydrolases[8] play a role in the conversion of cellulose to glucose by cutting the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Structurally, cellulases and xylanases frequently consist of a catalytic domain joined to a cellulose-binding domain (CBD) via a linker region that is rich in proline and/or hydroxy-amino acids. In type I exoglucanases, the CBD domain is found at the C-terminal extremity of these enzyme (this short domain forms a hairpin loop structure stabilised by 2 disulphide bridges).

References

This article incorporates text from the public domain Pfam and InterPro: IPR001722