ENZYMATIC CATALYSIS AND TRANSITION-STATE THEORY
ENZYMATIC CATALYSIS AND TRANSITION-STATE THEORY
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DOI：
10.1126/science.180.4082.149
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发表时间：
1973-01-01
期刊：
影响因子：
56.9
通讯作者：
LIENHARD, GE
中科院分区：
文献类型：
--
作者：
LIENHARD, GE
过渡态理论在酶催化中的应用提供了一种根据决定配体与蛋白质结合强度的因素来理解酶催化的方法。过渡态与酶的结合应该比底物更紧密地结合，这一预测得到了过渡态稳定类似物的实验结果的支持。过渡态类似物在理解酶催化和抑制酶方面具有巨大的应用潜力。由于它们作为酶抑制剂的效力和特异性，其中一些可能成为非常有用的化疗剂。
The application of transition-state theory to enzymatic catalysis provides an approach to understanding enzymatic catalysis in terms of the factors that determine the strength of binding of ligands to proteins. The prediction that the transition state should bind to the enzyme much more tightly than the substrate is supported by the experimental results with stable analogs of transition states. Transition-state analogs have great potential for use in understanding enzymatic catalysis and in inhibiting enzymes. Because of their potency and specificity as enzyme inhibitors, some of them may become very useful chemotherapeutic agents.