Research progress of the atypical kinetic profiles of cytochrome P450 enzymes.
- Author:
Cai-Wen ZENG
1
;
Fang HE
;
Chun-Hua XIA
;
Yu-Qing XIONG
Author Information
1. Institute of Clinical Pharmacology, Medical College of Nanchang University, Nanchang 330006, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Benzoflavones;
pharmacology;
Binding Sites;
Cytochrome P-450 CYP3A;
chemistry;
metabolism;
Cytochrome P-450 Enzyme System;
chemistry;
metabolism;
Enzyme Activation;
Humans;
Kinetics;
Protein Binding;
Substrate Specificity
- From:
Acta Pharmaceutica Sinica
2012;47(6):725-729
- CountryChina
- Language:Chinese
-
Abstract:
Cytochrome P450 enzymes are composed of many isozymes and involved in the biotransformation of both exogenous and endogenous substances. A growing number of studies have found that the P450 enzymes do not always follow the classical Michaelis-Menten kinetics, but show atypical kinetic behavior, which is also the current research hotspot. In this paper, the category and mechanisms of atypical kinetics of the P450 enzyme were reviewed, providing theoretical basis for the research of enzyme kinetics.
