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In molecular biology, glycoside hydrolase family 38 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 38 (CAZY GH_38 ) comprises enzymes with only one known activity; alpha-mannosidase () (). Lysosomal alpha-mannosidase is necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. The enzyme catalyzes the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides, and can cleave all known types of alpha-mannosidic linkages. Defects in the gene cause lysosomal alpha-mannosidosis (AM), a lysosomal storage disease characterised by the accumulation of unbranched oligo-saccharide chains. A domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase. ==References== 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Glycoside hydrolase family 38」の詳細全文を読む スポンサード リンク
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