Cytochrome P-450 : multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms

The carbon monoxide-binding pigment of liver microsomes was shown over 25 years ago to be a hemoprotein of the b type and, as judged by the photochemical action spectrum, to be involved in the oxidation of drugs and steroids. The solubilization and resolution of the components of this enzyme system...

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Bibliographic Details
Published in:The Journal of biological chemistry 1991-07, Vol.266 (21), p.13469-13472
Main Authors: PORTER, T. D, COON, M. J
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Catalysis
Cytochrome P-450 Enzyme System - chemistry
Cytochrome P-450 Enzyme System - genetics
Cytochrome P-450 Enzyme System - metabolism
cytochrome P450
DNA Mutational Analysis
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation
Humans
Isoenzymes - metabolism
isoforms
Oxidoreductases
Oxygen - metabolism
Peroxides - metabolism
regulation
reviews
Structure-Activity Relationship
Substrate Specificity
substrates
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Summary:The carbon monoxide-binding pigment of liver microsomes was shown over 25 years ago to be a hemoprotein of the b type and, as judged by the photochemical action spectrum, to be involved in the oxidation of drugs and steroids. The solubilization and resolution of the components of this enzyme system from microsomal membranes and the reconstitution of an active complex containing cytochrome P-450, NADPH-cytochrome P-450 reductase, and phosphatidylcholine permitted the purification and thorough characterization of these constituents. The aims of this review are to summarize briefly our current knowledge of the function, structure, mechanism of action, and regulation of this interesting group of catalysts and to describe recent progress in several areas where much still remains to be learned.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(18)92717-1