title: Function and structure studies of GH family 31 and 97 α-glycosidases.
abstract: A huge number of glycoside hydrolases are classified into the glycoside hydrolase family (GH family) based on their amino-acid sequence similarity. The glycoside hydrolases acting on α-glucosidic linkage are in GH family 4, 13, 15, 31, 63, 97, and 122. This review deals mainly with findings on GH family 31 and 97 enzymes. Research on two GH family 31 enzymes is described: clarification of the substrate recognition of Escherichia coli α-xylosidase, and glycosynthase derived from Schizosaccharomyces pombe α-glucosidase. GH family 97 is an aberrant GH family, containing inverting and retaining glycoside hydrolases. The inverting enzyme in GH family 97 displays significant similarity to retaining α-glycosidases, including GH family 97 retaining α-glycosidase, but the inverting enzyme has no catalytic nucleophile residue. It appears that a catalytic nucleophile has been eliminated during the molecular evolution in the same way as a man-made nucleophile mutant enzyme, which catalyzes the inverting reaction, as in glycosynthase and chemical rescue.
authors.affiliation: Research Faculty of Agriculture, Hokkaido University, Sapporo, Japan. okuyama@abs.agr.hokudai.ac.jp
authors.forename: Masayuki
authors.initials: M
authors.lastname: Okuyama
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004926:Escherichia coli / Q000201:enzymology; D019143:Evolution, Molecular; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D006026:Glycoside Hydrolases