Yagisawa S
School of Pharmaceutical Sciences, Nagasaki University, Japan.
Biochem J. 1995 May 15;308 ( Pt 1)(Pt 1):305-11. doi: 10.1042/bj3080305.
A comprehensive theory for relating free-energy profiles to kinetic equations of enzyme reactions has been developed. It enables expression of the overall rate and the concentrations of reaction intermediates in terms of the heights of peaks in free-energy profiles for various reactions. The reactions include consecutive reactions with intermittent irreversible steps, those with dead-end side reactions and completely reversible reactions. The usefulness of the theory is shown by analysis of a single-substrate reaction, a reaction with a covalent intermediate, and product inhibition in a two-substrate reaction, in which kinetic parameters such as Vmax and Km are related to the peak heights in free-energy profiles. The paper refers also to the concept of rate-determining step (RDS) and shows the utility of a related concept rate-determining zone (RDZ) which indicates the reaction steps between the main intermediate and the RDS. The concept of RDZ is useful for resolving confusion related to the concept of RDS. It should be emphasized that the present approach is applicable only to linear reactions.
已经建立了一种将自由能分布与酶反应动力学方程相关联的综合理论。它能够根据各种反应自由能分布中峰的高度来表达总速率和反应中间体的浓度。这些反应包括具有间歇性不可逆步骤的连续反应、具有死端副反应的反应以及完全可逆反应。通过分析单底物反应、具有共价中间体的反应以及双底物反应中的产物抑制，展示了该理论的实用性，其中诸如Vmax和Km等动力学参数与自由能分布中的峰高相关。本文还提到了速率决定步骤（RDS）的概念，并展示了相关概念速率决定区（RDZ）的效用，该区域指示了主要中间体和RDS之间的反应步骤。RDZ的概念有助于解决与RDS概念相关的混淆。应该强调的是，目前的方法仅适用于线性反应。
