Publication: Cytochrome P450s
1
Issued Date
2009
Resource Type
Language
eng
ISSN
0125-3611 (Print)
2651-0561 (Online)
2651-0561 (Online)
Rights Holder(s)
Office of Academic Affairs Faculty of Medicine Ramathibodi Hospital Mahidol University
Bibliographic Citation
Ramathibodi Medical Journal. Vol. 32, No. 2 (Apr-Jun 2009), 101-104
Suggested Citation
Amnuay Thithapandha, อำนวย ฐิตาพันธ์ Cytochrome P450s. Ramathibodi Medical Journal. Vol. 32, No. 2 (Apr-Jun 2009), 101-104. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/79892
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Cytochrome P450s
Author(s)
Abstract
Cytochrome P450s or CYPs are heme proteins found in several organs but in high amount in both mammalian and human livers. The heme iron binds oxygen in the CYP active site, where oxidation of xenobiotics and endogenous compounds occurs. Electrons are supplied by the enzyme NADPH-cyto- chrome P450 oxidoreductase and its cofactor, NADPH. Metabolism of a substrate by a CYP consumes one molecule of O2 and produces on oxidized substrate and a molecule of water (Fig. 1). Depending on the nature of the substrate, the reaction for some CYPs is partially “uncoupled,” consuming more Oz than substrate metabolized and producing “activated oxygen” or O2 which is usually converted to water by the enzyme superoxide dismutase (SOD).