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翻訳と辞書　辞書検索 [ 開発暫定版 ] スポンサード リンク Glycoside hydrolase family 65 ： ウィキペディア英語版 Glycoside hydrolase family 65 In molecular biology, glycoside hydrolase family 65 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. )〕 This family of glycosyl hydrolases ((CAZY GH_65 )) includes vacuolar acid trehalase and maltose phosphorylases. Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. It consists of three structural domains. The C-terminal domain forms a two layered jelly roll motif. This domain is situated at the base of the catalytic domain, however its function remains unknown. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom.〔 The catalytic domain also forms the majority of the dimerisation interface. The N-terminal domain is believed to be essential for catalytic activity〔 although its precise function remains unknown. ==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 65」の詳細全文を読む スポンサード リンク 翻訳と辞書 : 翻訳のためのインターネットリソース Copyright(C) kotoba.ne.jp 1997-2016. All Rights Reserved.