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Glucoamylase, glucodextranase, trehalase, and eukaryotic N-glycan processing α-glucosidase I have been identified as exo-acting enzymes that hydrolyze α-1,Xglucosidic linkages from the non-reducing end to produce β-glucose. While the physiological functions of these enzymes are different, they share a catalytic (α/α)6 barrel domain and show many structural similarities. These enzymes, with few exceptions, belong to the glycoside hydrolase families (GHs) 15, 37, and 63 in the CAZy database, and all these enzymes have 2 conserved aspartic or glutamic acid residues in the catalytic domain. The observations led us to consider that the group of GH15, GH37, and GH63 may be designated as a “glucoamylase family.” There are also many hydrolases and phosphorylases structurally related to GH15, GH37, and GH63. A. Introduction Glucose is one of the most essential molecules for living organisms, and it performs numerous physiological functions. For example, starch, a polysaccharide consisting of glucose residues, functions as an energy storage material, while in the eukaryotic N-glycans, processing of glucose residues is important for the calnexin/calreticulin binding cycle involved in protein folding and quality control (1–3). This multi-functionality of carbohydrates can be attributed to wide variety of glycosidic linkages. Monosaccahrides show 2 anomeric forms, namely αand β-forms; even if we consider only α-gluco-disaccharides, there are 5 disaccharides, trehalose, kojibiose, nigerose, maltose, and isomaltose, which are linked by α-1,1-, α-1,2-, α-1,3-, α-1,4-, and α-1,6glucocidic linkages, respectively. We are presently studying the enzymes that hydrolyze α-1,X-glucosidic linkages, and we have determined the デンプンに作用する酵素とN 結合型糖鎖に作用する酵素の構造上の相同性 : α -1,Xグルコシド 結合をエキソ型で加水分解しβ グルコースを生成する酵素

trends in glycoscience and glycotechnology

Structural Similarity between a Starch-hydrolyzing Enzyme and an N-Glycan-Hydrolyzing Enzyme: Exohydrolases Cleaving α-1,X-Glucosidic Linkages to Produce β-Glucose