α-Glucosidase Mutant Catalyzes"α-Glycosynthase"-type Reaction
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- OKUYAMA Masayuki
- <i>Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University</i>
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- MORI Haruhide
- <i>Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University</i>
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- WATANABE Kotomi
- <i>Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University</i>
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- KIMURA Atsuo
- <i>Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University</i>
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- CHIBA Seiya
- <i>Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University</i>
書誌事項
- タイトル別名
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- .ALPHA.-Glucosidase Mutant Catalyzes ".ALPHA.-Glycosynthase"-type Reaction.
- アルファ Glucosidase Mutant Catalyzes アルファ Glycosynthase type Reaction
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抄録
Replacement of the catalytic nucleophile Asp481 by glycine in Schizosaccharomyces pombe α-glucosidase eliminated the hydrolytic activity. The mutant enzyme (D481G) was found to catalyze the formation of an α-glucosidic linkage from β-glucosyl fluoride and 4-nitrophenyl (PNP) α-glucoside to produce two kinds of PNP α-diglucosides, α-isomaltoside and α-maltoside. The two products were not hydrolyzed by D481G, giving 41 and 29% yields of PNP α-isomaltoside and α-maltoside, respectively. PNP monoglycosides, such as α-xyloside, α-mannoside, or β-glucoside, acted as the substrate, but PNP α-galactoside and maltose could not. No detectable product was observed in the combination of α-glucosyl fluoride and PNP α-glucoside. This study is the first report on an “α-glycosynthase”-type reaction to form an α-glycosidic linkage.<br>
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 66 (4), 928-933, 2002
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206475237248
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- NII論文ID
- 110002693759
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- NII書誌ID
- AA10824164
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- COI
- 1:CAS:528:DC%2BD38XjsFaktrk%3D
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 6155828
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- PubMed
- 12036080
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可