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首页> 外文期刊>Biochemistry >Multiple conformational changes in enzyme catalysis.
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Multiple conformational changes in enzyme catalysis.

机译：酶催化的多种构象变化。

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摘要

Understanding the molecular mechanisms of enzyme catalysis and allosteric regulation has been a primary goal of biochemistry for many years. The dynamics of these processes, approached through a variety of kinetic methods, are discussed. The results obtained for many different enzymes suggest that multiple intermediates and conformations are general characteristics of the catalytic process and allosteric regulation. Ribonuclease, dihydrofolate reductase, chymotrypsin, aspartate aminotransferase, and aspartate transcarbamoylase are considered as specific examples. Typical and maximum rates of conformational changes and catalysis are also discussed, based on results obtained from model systems. The nature and rates of interconversion of the intermediates, along with structural information, can be used as the bases for understanding the incredible catalytic efficiency of enzymes. Potential roles of conformational changes in the catalytic process are discussed in terms of static and environmental effects, and in terms of dynamic coupling within the enzyme-substrate complex.
机译：了解酶催化和变构规则的分子机制是多年来生物化学的主要目标。讨论了通过各种动力学方法接近这些过程的动态。为许多不同酶获得的结果表明，多种中间体和构象是催化过程的一般特征和变构调控。核糖核酸酶，二氢酚酸还原酶，胰凝乳素，天冬氨酸氨基转移酶和天冬氨酸转基氨基酰基酶被认为是具体的实例。还讨论了根据模型系统获得的结果的结果讨论了典型和最大构象变化和催化率。中间体相互互连的性质和速率以及结构信息可用作理解酶令人难以置信的催化效率的基础。在静态和环境效应方面讨论了催化过程的构象变化的潜在作用，以及在酶 - 底物复合物内的动态偶联方面。

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