一种基于蛋白质构象弛豫的酶作用机制模型。

A model of the mechanism of enzyme action in terms of protein conformational relaxation.

作者信息

Averbukh I S, Blumenfeld L A, Kovarsky V A, Perelman N F

出版信息

Biochim Biophys Acta. 1986 Sep 26;873(2):290-6. doi: 10.1016/0167-4838(86)90056-7.

Abstract

A theoretical model of enzymatic reaction is formulated in which the modulation of the reaction coordinates by low-frequency conformational motions of the enzyme molecule causes the lowering of the activation energy barriers until they completely disappear. If the rates of electron transitions in the enzyme-substrate complex exceed the characteristic frequencies of conformational motions then the rate of the elementary enzymatic reaction shows hysteresis dependence on temperature and substrate concentration.

摘要

构建了一个酶促反应的理论模型，其中酶分子的低频构象运动对反应坐标的调制导致活化能垒降低，直至完全消失。如果酶 - 底物复合物中的电子跃迁速率超过构象运动的特征频率，那么基本酶促反应的速率对温度和底物浓度呈现滞后依赖性。