ATP-Dependent Inactivation of Escherichia coli γ-Glutamylcysteine Synthetase by L-Glutamic Acid γ-Monohydroxamate
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概要
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Incubation of Escherichia coli γ-glutamylcysteine synthetase with L-glutamic acid γ-monohydroxamate and ATP caused slow but irreversible inhibition of the enzyme, and more than 90% activity was lost in three days. The enzyme was not inactivated when ATP was absent or L-aspartic acid β-monohydroxamate was substituted for L-glutamic acid γ-monohydroxamate, suggesting that the inactivation process reflected a mechanism-based reaction of L-glutamic acid γ-monohydroxamate and ATP.
- 社団法人日本農芸化学会の論文
- 1998-07-23
著者
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Hiratake Jun
Institute For Chemical Research Kyoto University
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Katoh Makoto
Institute For Chemical Research Kyoto University
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Oda Junichi
Institute For Chemical Research Kyoto University
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