Chemical modification of histidyl residue in the active site of brewer's yeast .ALPHA.-glucosidase II.
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- SOMEYA Yoshiaki
- Department of Agricultural Chemistry, Faculty of Agriculture, Hokkaido University
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- MATSUI Hirokazu
- Department of Agricultural Chemistry, Faculty of Agriculture, Hokkaido University
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- CHIBA Seiya
- Department of Agricultural Chemistry, Faculty of Agriculture, Hokkaido University
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α-Glucosidase II from brewer's yeast was inactivated by photooxidation in the presence of rose bengal at pH 6.8. Addition of substrate diminished the rate of inactivation. During photoinactivation the Michaelis constant was unchanged, but the maximumvelocity decreased with a decrease in residual activity. Anamino acid analysis of the oxidized enzymeshowed the reduction of two histidines and the cysteine residues.<br> Inactivation of the α-glucosidase II by diethylpyrocarbonate was also observed. One histidyl residue was modified, but tyrosyl and cysteinyl residues were not affected. The loss of activity of the modified enzyme was restored by treatment with hydroxylamine.<br> These results suggest that at least one histidyl residue serves a catalytic function in brewer's yeast α-glucosidase II.
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 48 (4), 873-879, 1984
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
- 1390282681439992192
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- NII論文ID
- 130000026939
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- COI
- 1:CAS:528:DyaL2cXktF2ks7k%3D
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- ISSN
- 18811280
- 00021369
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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
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- 使用不可