Multiple conformational changes in enzyme catalysis
Multiple conformational changes in enzyme catalysis
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DOI：
10.1021/bi0260839
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发表时间：
2002-07-02
期刊：
影响因子：
2.9
通讯作者：
Hammes, GG
中科院分区：
文献类型：
--
作者：
Hammes, GG
多年来，了解酶催化和变构调节的分子机制一直是生物化学的主要目标。通过各种动力学方法对这些过程的动力学进行了讨论。对许多不同的酶所获得的结果表明，多个中间体和构象是催化过程和变构调节的一般特征。核糖核酸酶、二氢叶酸还原酶、糜蛋白酶、天冬氨酸氨基转移酶和天冬氨酸转氨酶被认为是具体的例子。基于从模型体系获得的结果，还讨论了构象变化和催化的典型和最大速率。中间体的相互转化的性质和速率，以及结构信息，可以作为理解酶令人难以置信的催化效率的基础。根据静态和环境效应以及酶-底物复合体中的动态耦合，讨论了构象变化在催化过程中的潜在作用。
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.