Effect of desdanine on nucleoside diphosphate kinase and pyruvate kinase of Escherichia coli.
Effect of desdanine on nucleoside diphosphate kinase and pyruvate kinase of Escherichia coli.
复制标题
地丹宁对大肠杆菌核苷二磷酸激酶和丙酮酸激酶的影响。
DOI：
10.7164/antibiotics.28.974
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发表时间：
1975
期刊：
影响因子：
--
通讯作者：
H. Umezawa
中科院分区：
文献类型：
--
作者：
T. Saeki;M. Hori;H. Umezawa
Kinetic analysis demonstrated that the irreversible inhibition of nucleoside diphosphate kinase of Escherichia coli by desdanine proceeds via a reversible Enzyme-Inhibitor complex. It is known that pyruvate kinase of E. coli becomes inactive upon prolonged dialysis in the absence of a reducing reagent, such as dithiothreitol and that the inactive enzyme is reactivated if dithiothretiol is added. Desdanine inhibits this reactivation process. The effect is discussed in relation to inhibition in relation to the inhibition of growth of E. coli by desdanine under anaerobic conditions. Pyruvate kinase of E. coli changes not only in intracellular quantity but in its kinetic characteristics depending on growth conditions, aerobic or anaerobic. The enzyme shows a broad specificity for nucleside diphosphates, especially in the presence of AMP, and thus resembles closely nucleoside diphosphate kinase. The in vivo role of pyruvate kinase in supplying nucleoside triphosphates under anaerobic conditions is discussed.
