组氨醇脱氢酶机制的稳态研究。
Steady-state investigations of the mechanism of histidinol dehydrogenase.
作者信息
Görisch H
出版信息
Biochem J. 1979 Jul 1;181(1):153-7. doi: 10.1042/bj1810153.
Abstract
Initial velocities of the histidinol dehydrogenase reaction (EC 1.1.1.23) were measured as a function of the concentrations of the substrates histidinol and NAD+ and in the presence and absence of the product NADH. The data are consistent with a Bi Uni Uni Bi Ping Pong mechanism. The kinetic constants of this mechanism were determined; Km for histidinol was found to be 14 microM and for NAD+ 0.7 mV; Ki for NAD+ was 0.4 mM.
摘要
测定了组氨醇脱氢酶反应（EC 1.1.1.23）的初始速度，该速度是底物组氨醇和NAD⁺浓度的函数，并且在有和没有产物NADH的情况下进行了测定。数据符合双底物双产物乒乓机制。确定了该机制的动力学常数；组氨醇的Km为14 μM，NAD⁺的Km为0.7 mV；NAD⁺的Ki为0.4 mM。
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