Effects of posttranslational modification on the activity of cytochrome P450: current progress.
- Author:
Yu-hua LI
1
;
Hui-chang BI
;
Min HUANG
Author Information
1. Lab of Drug Metabolism & Pharmacokinetics, School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Cytochrome P-450 Enzyme System;
genetics;
metabolism;
Glycosylation;
Humans;
Nitric Oxide;
metabolism;
Oxidation-Reduction;
Phosphorylation;
Protein Processing, Post-Translational;
RNA, Messenger;
metabolism;
Ubiquitination
- From:
Acta Pharmaceutica Sinica
2011;46(5):487-492
- CountryChina
- Language:Chinese
-
Abstract:
Regulation of the activity of CYP450 has always been research focus of drug metabolism. The effect of compounds on the mRNA and protein expression level of CYP450 is the main purpose of most of the existing reports. In recent years, the protein modification in the posttranslation level has been found to participate in maintaining the proper function of CYP450, thus effect of posttranslational modification on the enzyme activity has been paid more and more attention. Posttranslational modifications including phosphorylation, nitration, and ubiquitination have been described to regulate the activity of CYP450. In this paper, recent developments in the effects of posttranslational modifications on the activity of CYP450 have been reviewed.
