M
Masayuki Okuyama
Researcher at Hokkaido University
Publications - 114
Citations - 2100
Masayuki Okuyama is an academic researcher from Hokkaido University. The author has contributed to research in topics: Hydrolase & Glycoside hydrolase. The author has an hindex of 24, co-authored 105 publications receiving 1756 citations. Previous affiliations of Masayuki Okuyama include Epson.
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Journal ArticleDOI
Structural and Functional Analysis of a Glycoside Hydrolase Family 97 Enzyme from Bacteroides thetaiotaomicron
Momoyo Kitamura,Masayuki Okuyama,Fumiko Tanzawa,Haruhide Mori,Yu Kitago,Nobuhisa Watanabe,Atsuo Kimura,Isao Tanaka,Min Yao +8 more
TL;DR: Major similarity between the catalytic domain of SusB and those of α-retaining glycoside hydrolases belonging to GH27, -36, and -31 despite the differences in catalytic mechanism was revealed.
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In vitro antiproliferative/cytotoxic activity on cancer cell lines of a cardanol and a cardol enriched from Thai Apis mellifera propolis
Dungporn Teerasripreecha,Preecha Phuwapraisirisan,Songchan Puthong,Kiyoshi Kimura,Masayuki Okuyama,Haruhide Mori,Atsuo Kimura,Chanpen Chanchao +7 more
TL;DR: This is the first report that Thai A. mellifera propolis contains at least two potentially new compounds (a cardanol and a cardol) with potential anti-cancer bioactivity, which could be alternative antiproliferative agents for future development as anti- cancer drugs.
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Molecular Basis for the Recognition of Long-chain Substrates by Plant α-Glucosidases
TL;DR: The crystal structure and mutational analyses of sugar beet α-glucosidase revealed its substrate binding properties and the long-substrate specificity was described as the N-loop and subdomain b2, which is an additional element inserted into the (β/α)8 barrel domain.
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α-Glucosidase Mutant Catalyzes “α-Glycosynthase”-type Reaction
TL;DR: In this article, a mutant enzyme (D481G) was found to catalyze the formation of an alpha-glucosidic linkage from beta-glocosyl fluoride and 4-nitrophenyl (PNP) alpha-Glucoside to produce two kinds of PNP alpha-diglucosides, alpha-isomaltoside and alpha-maltose.
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Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α‐glucosidase from Schizosaccharomyces pombe
TL;DR: The carboxyl group (-COOH) of the Asp647 residue was for the first time shown to be the most likely proton donor acting as the acid catalyst in the alpha-glucosidase of family II, although the role of the Glu484 residue remains obscure.