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・ Glycoside hydrolase family 100
・ Glycoside hydrolase family 101
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・ Glycoside hydrolase family 11
・ Glycoside hydrolase family 12
・ Glycoside hydrolase family 13
・ Glycoside hydrolase family 14
・ Glycoside hydrolase family 15
・ Glycoside hydrolase family 16
・ Glycoside hydrolase family 17
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・ Glycoside hydrolase family 19
・ Glycoside hydrolase family 2
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Glycoside hydrolase family 24
・ Glycoside hydrolase family 25
・ Glycoside hydrolase family 26
・ Glycoside hydrolase family 27
・ Glycoside hydrolase family 28
・ Glycoside hydrolase family 29
・ Glycoside hydrolase family 3
・ Glycoside hydrolase family 30
・ Glycoside hydrolase family 31
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Glycoside hydrolase family 24 : ウィキペディア英語版
Glycoside hydrolase family 24

In molecular biology, glycoside hydrolase family 24 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 24 (CAZY GH_24 ) comprises enzymes with only one known activity; lysozyme (). This family includes lambda phage lysozyme and ''Escherichia coli'' endolysin. Lysozyme helps to release mature phage particles from the cell wall by breaking down the peptidoglycan. The enzyme hydrolyses the 1,4-beta linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of prokaryotic cell walls. ''E. coli'' endolysin also functions in bacterial cell lysis and acts as a transglycosylase. The T4 lysozyme structure contains 2 domains, the interface between which forms the active-site cleft. The N-terminus of the 2 domains undergoes a 'hinge-bending' motion about an axis passing through the molecular waist.〔 This mobility is thought to be important in allowing access of substrates to the enzyme active site.
== References ==


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