Suicide Substrate-based Inactivation of Endodextranase by .OMEGA.-Epoxyalkyl .ALPHA.-D-Glucopyranosides
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- Kang Hee-Kwon
- Research Faculty of Agriculture, Hokkaido University
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- Kim Young-Min
- Research Faculty of Agriculture, Hokkaido University
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- Nakai Hiroyuki
- Research Faculty of Agriculture, Hokkaido University
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- Kang Min-Sun
- Research Faculty of Agriculture, Hokkaido University
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- Hakamada Wataru
- College of Bioresource Sciences, Nihon University
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- Okuyama Masayuki
- Research Faculty of Agriculture, Hokkaido University
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- Mori Haruhide
- Research Faculty of Agriculture, Hokkaido University
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- Nishio Toshiyuki
- College of Bioresource Sciences, Nihon University
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- Kimura Atsuo
- Research Faculty of Agriculture, Hokkaido University
Bibliographic Information
- Other Title
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- ω-エポキシアルキルα-<small>D</small>-グルコピラノシドによるエンド型デキストラナーゼの自殺基質型失活
- Suicide substrate-based inactivation of endodextranase by ω-epoxyalkyl α-D-glucopyranosides
- Suicide substrate based inactivation of endodextranase by o epoxyalkyl a D glucopyranosides
- Suicide substrate-based inactivation of endodextranase by ω-epoxyalkyl α-glucopyranosides
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Abstract
Three kinds of ω-epoxyalkyl α-glucopyranosides (3′,4′-epoxybutyl α-D-glucopyranoside (E4G), 4′,5′-epoxypentyl α-D-glucopyranoside (E5G) and 5′,6′-epoxyhexyl α-D-glucopyranoside (E6G)), having alkyl chains of different lengths at their aglycone moieties, inactivated the endodextranase from Streptococcus mutans ATCC 25175 (SmDex) irreversibly with the pseudo-first order kinetics. Alkyl chain length-dependent inactivation was observed and the degree of activity loss was E5G, E6G and E4G, in that order, implying that the distance between epoxide group and glucosyl residue of ω-epoxyalkyl α-glucopyranoside was important in the modification of endodextranase. Inactivation by E5G followed the model of reversible intermediate-complex formation mechanism (suicide inhibitor-based mechanism). The rate constant of irreversible inactivation (k) and the dissociation constant of intermediate-complex (KR) of SmDex and E5G were 0.44 min-1 and 1.45 mM, respectively. Hydrolytic reaction product (isomaltose) protected SmDex from E5G-inactivation, suggesting that E5G bound to the catalytic site of SmDex. This is the first report that ω-epoxyalkyl α-glucopyranoside becomes a suicide substrate for endodextranase.
Journal
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 57 (4), 269-272, 2010
The Japanese Society of Applied Glycoscience
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Details 詳細情報について
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- CRID
- 1390001206293081600
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- NII Article ID
- 10026967780
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- NII Book ID
- AN10453916
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- ISSN
- 18807291
- 13447882
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- NDL BIB ID
- 10875307
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- Text Lang
- en
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- Data Source
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- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed