一种用于低催化活性酶动力学分析的线性化方法。

A linearization method for low catalytic activity enzyme kinetic analysis.

作者信息

Toti Paolo, Petri Antonella, Pelaia Valerio, Osman Ahmed M, Paolini Moreno, Bauer Carlo

机构信息

Department of Physiology and Biochemistry, Biochemistry Unit, University of Pisa, Italy.

出版信息

Biophys Chem. 2005 Apr 22;114(2-3):245-51. doi: 10.1016/j.bpc.2004.12.043. Epub 2005 Jan 5.

DOI:10.1016/j.bpc.2004.12.043

PMID:15829359

Abstract

A kinetic analysis was made and a linear plot based on the general rate equation derived by Laidler [Can. J. Chem. 33, 1614-1624] is proposed. This linearization method allows determining the kinetic parameters (K(m), k(cat)) and E for enzymes with low catalytic activity. The method was applied to chloroperoxidase from Caldariomyces fumago [EC 1.11.1.10], whose kinetic parameters K(m)(app), k(cat)(app), and E with monochlorodimedone as substrate, were obtained by using the linearization plot and the V(max) value (calculated by Eadie-Hofstee plot). This plot could also be useful to the study of abenzyme kinetics provided the concentration of the latter is either higher or equal than K(m) value.

摘要

进行了动力学分析，并提出了基于莱德勒[《加拿大化学杂志》33, 1614 - 1624]推导的一般速率方程的线性图。这种线性化方法允许确定具有低催化活性的酶的动力学参数（K(m)，k(cat)）和E。该方法应用于烟曲霉氯过氧化物酶[EC 1.11.1.10]，通过使用线性化图和V(max)值（由伊迪 - 霍夫斯泰图计算）获得了以一氯二甲基酮为底物时其动力学参数K(m)(app)、k(cat)(app)和E。如果酶的浓度高于或等于K(m)值，该图对于研究酶动力学也可能有用。