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[胰凝乳蛋白酶催化中自由能线性原理]

[Principle of free energies linearity in chymotrypsin catalysis].

作者信息

Kozlov L V

出版信息

Biokhimiia. 1979 Jan;44(1):166-71.

PMID:33727
Abstract

The applicability of the previously described principle of free energies linearity for semispecific substrates of chymotrypsin for the derivatives of acetylphenylalanine, acetyltryptophane and acetyltyrosine was demonstrated. The pH dependence of the parameters of a linear equation describing the relationship between the free energy of hydrolysis and the logarithmus of the kcat/Km(app) ratio suggests that at optimal pH the stability of the activation barrier of enzyme acetylation for all semispecific substrates is observed.

摘要

已证明先前描述的自由能线性原理适用于胰凝乳蛋白酶对乙酰苯丙氨酸、乙酰色氨酸和乙酰酪氨酸衍生物的半特异性底物。描述水解自由能与kcat/Km(app)比值对数之间关系的线性方程参数的pH依赖性表明,在最佳pH值下,观察到所有半特异性底物的酶乙酰化活化屏障的稳定性。

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1
[Principle of free energies linearity in chymotrypsin catalysis].[胰凝乳蛋白酶催化中自由能线性原理]
Biokhimiia. 1979 Jan;44(1):166-71.
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Biochemistry. 1998 Aug 25;37(34):11940-8. doi: 10.1021/bi980278s.
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