Inactivation of Wheat Dihydrodipicolinate Synthase by 3-Bromopyruvate
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概要
- 論文の詳細を見る
When added directly to the assay medium under standard conditions, 3-bromopyruvate inhibited wheat dihydrodipicolinate synthase (DHDPS) competitively with respect to pyruvate and uncompetitively with respect to aspartate semialdehyde. When DHDPS was incubated with 3-bromopyruvate at pH 7.5 and 30°C, this reagent irreversibly inactivated the enzyme. The inactivation followed pseudofirst-order kinetics during the early period of inactivation; then the inactivation rate decreased. For the early period of inactivation, the pseudo-first-order rate constant was 0.29 min-1 and the Ki of 3-bromopyruvate was 1.8mM. Pyruvate protected against inactivation, while aspartate semialdehyde partially did so and lysine did not. The Hill constant for lysine of the enzyme inactivated by 73 % was about half of that of the untreated enzyme.
- 社団法人 日本農芸化学会の論文
著者
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Kumpaisal Rosarin
Research Center For Cell And Tissue Culture Faculty Of Agriculture Kyoto University
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HASHIMOTO Takashi
Research and Education Center for Genetic Information, Nara Institute of Science and Technology
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YAMADA Yasuyuki
Research Center for Ceil and Tissue Culture, Faculty of Agriculture, Kyoto University
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