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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Eur J Biochem. 1976 Jul 1;66(2):401-4. doi: 10.1111/j.1432-1033.1976.tb10529.x.

The rate constants for NADH binding and dissociation for carboxymethylated alcohol dehydrogenase have been determined and compared to those for the native enzyme. 2. Steady-state and transient kinetic experiments have shown that the hydrogen transfer step is rate-determining for oxidation of ethanol by carboxymethylated alcohol dehydrogenase. The rate constant of 0.19 s-1 is considerably slower than that for the native enzyme. 3. The steady-state parameter, V/[E], was obtained for each of a series of alcohols and correlated with the Taft sigma parameter. The linear relationship obtained indicates that the same step, hydrogen transfer, is rate-determining for all the alcohols. The sigma value obtained is the same as for the native enzyme; the implications of this for the mechanism of hydrogen transfer are discussed.

已测定羧甲基化乙醇脱氢酶与NADH结合和解离的速率常数，并与天然酶的相应常数进行了比较。2. 稳态和瞬态动力学实验表明，氢转移步骤是羧甲基化乙醇脱氢酶氧化乙醇的速率决定步骤。0.19 s⁻¹的速率常数比天然酶的速率常数慢得多。3. 获得了一系列醇类各自的稳态参数V/[E]，并将其与塔夫脱σ参数相关联。得到的线性关系表明，对于所有醇类，相同的步骤即氢转移是速率决定步骤。得到的σ值与天然酶的相同；讨论了其对氢转移机制的影响。

Eur J Biochem. 1976 Jul 1;66(2):401-4. doi: 10.1111/j.1432-1033.1976.tb10529.x.

The rate constants for NADH binding and dissociation for carboxymethylated alcohol dehydrogenase have been determined and compared to those for the native enzyme. 2. Steady-state and transient kinetic experiments have shown that the hydrogen transfer step is rate-determining for oxidation of ethanol by carboxymethylated alcohol dehydrogenase. The rate constant of 0.19 s-1 is considerably slower than that for the native enzyme. 3. The steady-state parameter, V/[E], was obtained for each of a series of alcohols and correlated with the Taft sigma parameter. The linear relationship obtained indicates that the same step, hydrogen transfer, is rate-determining for all the alcohols. The sigma value obtained is the same as for the native enzyme; the implications of this for the mechanism of hydrogen transfer are discussed.

已测定羧甲基化乙醇脱氢酶与NADH结合和解离的速率常数，并与天然酶的相应常数进行了比较。2. 稳态和瞬态动力学实验表明，氢转移步骤是羧甲基化乙醇脱氢酶氧化乙醇的速率决定步骤。0.19 s⁻¹的速率常数比天然酶的速率常数慢得多。3. 获得了一系列醇类各自的稳态参数V/[E]，并将其与塔夫脱σ参数相关联。得到的线性关系表明，对于所有醇类，相同的步骤即氢转移是速率决定步骤。得到的σ值与天然酶的相同；讨论了其对氢转移机制的影响。