イソマルトデキストラナーゼのサブサイト親和力の評価
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- Takayanagi Tsutomu
- Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University
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- Kimura Atsuo
- Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University
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- Matsui Hirokazu
- Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University
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- Okada Gentaro
- Department of Biology, Faculty of Education, Shizuoka University
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- Chiba Seiya
- Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University
書誌事項
- タイトル別名
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- Evaluation of Subsite Affinities of Isomalto-dextranase from Arthrobacter globiformis.
この論文をさがす
抄録
The subsite affinities of isomalto-dextranase (EC 3.2.1.94) from a soil bacterium, Arthrobacter globiformis T6 were evaluated to be>7.3, <-7.2, 6.7, 0.74 and 0.18 kcal/mol for subsites 1, 2, 3, 4 and 5, respectively, from the rate parameters (Km and k0) for the hydrolyses of isomalto-triose, -tetraose, -pentaose, -hexaose, -heptaose and -octaose. The intrinsic rate constant (kint) was calculated to be 3.1×102 s-1. Subsites 1 and 3, showing large affinity values, were thought to attract the substrate and to form the productive binding. Isopanose and maltotriose without α-isomaltosyl unit in their non-reducing ends acted neither as substrate nor as inhibitor for the isomaltodextranase, while the enzyme hydrolyzed oligosaccharides with α-isomaltosyl unit in their nonreducing ends. From these results, it was suggested that the binding of the α-isomaltosyl unit in the non-reducing end to subsites 1 and 2 was essential for the formation of the productive bindings be tween the substrates and the enzyme.
収録刊行物
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 49 (2), 123-127, 2002
日本応用糖質科学会
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詳細情報 詳細情報について
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- CRID
- 1390001206293528576
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- NII論文ID
- 10008253510
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- NII書誌ID
- AN10453916
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- ISSN
- 13403494
- 18807291
- 13447882
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- NDL書誌ID
- 6142347
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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
- IRDB
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可