Glycoside hydrolase family 39

Glycosyl hydrolases family 39

crystal structure of beta-d-xylosidase from thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase
Identifiers
Symbol Glyco_hydro_39
Pfam PF01229
Pfam clan CL0058
InterPro IPR000514
PROSITE PDOC00787
SCOP 1uhv
SUPERFAMILY 1uhv
CAZy GH39

In molecular biology, glycoside hydrolase family 39 is a family of glycoside hydrolases.

Glycoside hydrolases EC 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 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(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[5]

Glycoside hydrolase family 39 CAZY GH_39 comprises enzymes with several known activities; alpha-L-iduronidase (EC 3.2.1.76); beta-xylosidase (EC 3.2.1.37).

The most highly conserved regions in these enzymes are located in their N-terminal sections. These contain a glutamic acid residue which, on the basis of similarities with other families of glycosyl hydrolases,[6] probably acts as the proton donor in their catalytic mechanism.

References

This article incorporates text from the public domain Pfam and InterPro IPR000514

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