Jump to main content
Jump to site search

Issue 9, 2013
Previous Article Next Article

Understanding the mechanism of cytochrome P450 3A4: recent advances and remaining problems

Author affiliations

Abstract

Cytochromes P450 (CYPs) represent a diverse group of heme-thiolate proteins found in almost all organisms. CYPs share a common protein fold but differ in substrate selectivity and catalyze a wide variety of monooxygenation reactions via activation of molecular oxygen. Among 57 human P450s, the 3A4 isoform (CYP3A4) is the most abundant and the most important because it metabolizes the majority of administered drugs. A remarkable feature of CYP3A4 is its extreme promiscuity in substrate specificity and cooperative substrate binding, which often leads to undesirable drugdrug interactions and toxic side effects. Owing to its importance in drug development and therapy, CYP3A4 has been the most extensively studied mammalian P450. In this review we provide an overview on recent progress and remaining problems in the CYP3A4 research.

Graphical abstract: Understanding the mechanism of cytochrome P450 3A4: recent advances and remaining problems

Back to tab navigation

Publication details

The article was received on 10 Aug 2012, accepted on 07 Sep 2012 and first published on 10 Sep 2012


Article type: Perspective
DOI: 10.1039/C2DT31833D
Citation: Dalton Trans., 2013,42, 3116-3126
  •   Request permissions

    Understanding the mechanism of cytochrome P450 3A4: recent advances and remaining problems

    I. F. Sevrioukova and T. L. Poulos, Dalton Trans., 2013, 42, 3116
    DOI: 10.1039/C2DT31833D

Search articles by author

Spotlight

Advertisements