Trivić S, Leskovac V
Faculty of Sciences, Novi Sad, Yugoslavia.
Indian J Biochem Biophys. 1994 Oct;31(5):387-91.
The kinetic mechanism of yeast alcohol dehydrogenase (EC 1.1.1.1) activity with the redox pair 2-propanol/acetone has been probed in detail by the application of initial rate studies in the absence and in the presence of products, and a dead-end inhibitor pyrazole. An overall steady-state random Bi Bi mechanism in both directions, with the formation of both abortive ternary complexes, enzyme.NADH.2-propanol and enzyme.NAD+.acetone has been observed. A complete list of steady-state kinetic constants are also reported for the redox pair (S)-(+)-2-butanol/2-butanone.
通过在不存在和存在产物以及一种终产物抑制剂吡唑的情况下进行初速率研究，详细探究了酵母乙醇脱氢酶（EC 1.1.1.1）与氧化还原对2-丙醇/丙酮反应的动力学机制。观察到在两个方向上均存在一个总体稳态随机双双机制，同时形成了两种无效三元复合物，即酶·NADH·2-丙醇和酶·NAD⁺·丙酮。还报告了氧化还原对（S）-（+）-2-丁醇/2-丁酮的稳态动力学常数的完整列表。
