Lin S X, Chou K C, Wong J T
Biochem J. 1982 Oct 1;207(1):179-81. doi: 10.1042/bj2070179.
By analysing the variations of saturation velocity and Michaelis constant with temperature and invoking the mathematical constraint represented by the Arrhenius equation, it becomes possible to estimate k+2 and indistinguishably k+1 and k-1 for the Michaelis--Menten mechanism of one-substrate enzyme reactions. Distinction between k+1 and k-1 may be obtained through the determination of isotopic rate effects. This procedure thus provides a basis for evaluating all three rate constants of the one-substrate mechanism, and disproves the suggestion that k+1 and k-1 are intrinsically unobtainable from steady-state kinetic measurements.
通过分析饱和速度和米氏常数随温度的变化，并引入由阿伦尼乌斯方程表示的数学约束，就有可能估计单底物酶反应的米氏-门坦机制中的k+2，以及难以区分的k+1和k-1。k+1和k-1之间的区分可以通过测定同位素速率效应来实现。因此，该方法为评估单底物机制的所有三个速率常数提供了基础，并反驳了认为k+1和k-1本质上无法从稳态动力学测量中获得的观点。
