H
IPR037019

Glycoside hydrolase family 7, catalytic domain superfamily

InterPro entry
Short nameGlyco_hydro_7_sf
Overlapping entries
 

Description

O-Glycosyl hydrolases (
3.2.1.
) 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 glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families
[2, 3]
. This classification is available on the CAZy (CArbohydrate-Active EnZymes) website.

Glycoside hydrolase family 7
GH7
comprises enzymes with several known activities; endoglucanase (
3.2.1.4
) and cellobiohydrolase (
3.2.1.91
). These enzymes were formerly known as cellulase family C.

Exoglucanases and cellobiohydrolases
[1]
play a role in the conversion of cellulose to glucose by cutting the dissaccharide cellobiose from the nonreducing end of the cellulose polymer chain. Structurally, cellulases and xylanases generally 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).

This entry represents the catalytic core domain of these enzymes
[4]
.

References

1.Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families. Gilkes NR, Henrissat B, Kilburn DG, Miller RC Jr, Warren RA. Microbiol. Rev. 55, 303-15, (1991). View articlePMID: 1886523

2.Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G. Proc. Natl. Acad. Sci. U.S.A. 92, 7090-4, (1995). View articlePMID: 7624375

3.Structures and mechanisms of glycosyl hydrolases. Davies G, Henrissat B. Structure 3, 853-9, (1995). View articlePMID: 8535779

4.The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes. Kleywegt GJ, Zou JY, Divne C, Davies GJ, Sinning I, Stahlberg J, Reinikainen T, Srisodsuk M, Teeri TT, Jones TA. J. Mol. Biol. 272, 383-97, (1997). View articlePMID: 9325098

GO terms

Cross References

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