Garrido-del Solo C, García-Cánovas F, Havsteen B H, Valero E, Varón R
Departamento de Química-Física, Universidad de Castilla-La Mancha, Albacete, Spain.
Biochem J. 1994 Oct 15;303 ( Pt 2)(Pt 2):435-40. doi: 10.1042/bj3030435.
A kinetic analysis of the Michaelis-Menten mechanism has been made for the case in which both the enzyme-substrate complex and the product are unstable or only the product is unstable, either spontaneously or as the result of the addition of a reagent. This analysis allows the derivation of equations which under conditions of limiting enzyme concentration relate the concentration of all of the species to the time. A kinetic data analysis is suggested, which leads to the evaluation of the kinetic parameters involved in the reaction. The analysis is based on the equation which describes the formation of products with time and one's experimental progress curves. We demonstrate the method numerically by computer simulation of the reaction with added experimental errors and experimentally by the use of data from the kinetic study of the action of tyrosinase on dopamine.
针对酶 - 底物复合物和产物均不稳定或仅产物不稳定的情况（不稳定情况可能是自发的，也可能是添加试剂的结果），对米氏机制进行了动力学分析。该分析可推导得出在酶浓度受限条件下将所有物种浓度与时间相关联的方程。本文提出了一种动力学数据分析方法，可用于评估反应中涉及的动力学参数。该分析基于描述产物随时间形成的方程以及实验得到的进程曲线。我们通过添加实验误差对反应进行计算机模拟，从数值上证明了该方法，并通过使用酪氨酸酶作用于多巴胺的动力学研究数据进行实验验证。
