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一项关于酵母乙醇脱氢酶与多种底物的动力学及作用机制的研究。

A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates.

作者信息

Dickinson F M, Monger G P

出版信息

Biochem J. 1973 Feb;131(2):261-70. doi: 10.1042/bj1310261.

Abstract
  1. The kinetics of oxidation of ethanol, propan-1-ol, butan-1-ol and propan-2-ol by NAD(+) and of reduction of acetaldehyde and butyraldehyde by NADH catalysed by yeast alcohol dehydrogenase were studied. 2. Results for the aldehyde-NADH reactions are consistent with a compulsory-order mechanism with the rate-limiting step being the dissociation of the product enzyme-NAD(+) complex. In contrast the results for the alcohol-NAD(+) reactions indicate that some dissociation of coenzyme from the active enzyme-NAD(+)-alcohol ternary complexes must occur and that the mechanism is not strictly compulsory-order. The rate-limiting step in ethanol oxidation is the dissociation of the product enzyme-NADH complex but with the other alcohols it is probably the catalytic interconversion of ternary complexes. 3. The rate constants describing the combination of NAD(+) and NADH with the enzyme and the dissociations of these coenzymes from binary complexes with the enzyme were measured.
摘要
  1. 研究了酵母醇脱氢酶催化下,NAD(+)氧化乙醇、丙醇-1、丁醇-1和丙醇-2的动力学,以及NADH还原乙醛和丁醛的动力学。2. 醛-NADH反应的结果与强制顺序机制一致,限速步骤是产物酶-NAD(+)复合物的解离。相比之下,醇-NAD(+)反应的结果表明,辅酶必须从活性酶-NAD(+)-醇三元复合物中发生一些解离,且该机制并非严格的强制顺序。乙醇氧化中的限速步骤是产物酶-NADH复合物的解离,但对于其他醇类,限速步骤可能是三元复合物的催化相互转化。3. 测量了描述NAD(+)和NADH与酶结合以及这些辅酶从与酶的二元复合物中解离的速率常数。

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