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Glycoside hydrolase family 108
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Glycoside hydrolase family 108 : ウィキペディア英語版
Glycoside hydrolase family 108

In molecular biology, glycoside hydrolase family 108 is a family of glycoside hydrolases.
Glycoside hydrolases 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.〔(Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999. )〕 This classification is available on the CAZy(http://www.cazy.org/GH1.html) web site,〔(Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999. )〕 and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.〔(CAZypedia, an online encyclopedia of carbohydrate-active enzymes. )〕
Glycoside hydrolase family 108 (CAZY GH_108 ) includes enzymes with lysozyme (N-acetylmuramidase) activity. A glutamic acid residue within a conserved Glu-Gly-Gly-Tyr motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion.
==References==


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