Inhibition of Soybean β-Amylase-Catalyzed Hydrolysis with Maltobionolactone
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- KOHNO Motoko
- Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University
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- NITTA Yasunori
- Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University
Bibliographic Information
- Other Title
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- マルトビオノラクトンによる大豆β-アミラーゼ水解反応の阻害
- Inhibition of Soybean ベータ Amylase Catal
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Abstract
The reversible conversion between maltobionolactone and maltobionic acid was analyzed kinetically; the rate constants were determined at each pH, and the pKa of maltobionic acid was estimated to be 3.60±0.02. The inhibition by maltobionolactone for the hydrolysis of soluble starch was inves tigated at pH 5.4 and 25t, and it was found that maltobionolactone was a competitive inhibitor with a K1 of 0.40 mNi. The unitary binding affinity (7.0 kcal?mol-1) was the same as that of maltotetraose (a substrate). From the result, taking the subsite affinities of this enzyme into account, it was presumed that maltobionolactone consisting of a gluconolactone, with half-chair or sofa conformation, and a glucose (Cl form) is a transition state analogue and binds at subsites 1 and 2.
Journal
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- Journal of Applied Glycoscience
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Journal of Applied Glycoscience 43 (2), 161-165, 1996
The Japanese Society of Applied Glycoscience
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Details 詳細情報について
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- CRID
- 1390001205171803648
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- NII Article ID
- 10008255305
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- NII Book ID
- AN10453916
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- COI
- 1:CAS:528:DyaK28XkvVGnu7s%3D
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- ISSN
- 18844898
- 13403494
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- NDL BIB ID
- 3995010
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- Data Source
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- JaLC
- NDL
- CiNii Articles
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- Abstract License Flag
- Disallowed