CYTOCHROME P450: Nature's Most Versatile Biological Catalyst
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- 22 September 2005
- journal article
- review article
- Published by Annual Reviews in Annual Review of Pharmacology and Toxicology
- Vol. 45 (1) , 1-25
- https://doi.org/10.1146/annurev.pharmtox.45.120403.100030
Abstract
▪ Abstract The author describes studies that led to the resolution and reconstitution of the cytochrome P450 enzyme system in microsomal membranes. The review indicates how purification and characterization of the cytochromes led to rigorous evidence for multiple isoforms of the oxygenases with distinct chemical and physical properties and different but somewhat overlapping substrate specificities. Present knowledge of the individual steps in the P450 and reductase reaction cycles is summarized, including evidence for the generation of multiple functional oxidants that may contribute to the exceptional diversity of the reactions catalyzed.Keywords
This publication has 108 references indexed in Scilit:
- Centrilobular expression of ethanol-inducible cytochrome P-450 (IIE1) in rat liverBiochemical and Biophysical Research Communications, 1988
- The P450 Gene Superfamily: Recommended NomenclatureDNA, 1987
- Isolation and characterization of a novel cytochrome P-450-like pseudogeneBiochemical and Biophysical Research Communications, 1986
- Properties of the tryptophan residue in rabbit liver microsomal cytochrome P-450 isozyme 2 as determined by fluorescenceBiochemical and Biophysical Research Communications, 1985
- Purification and properties of P-450lm3b, a constitutive form of cytochrome P-450, from rabbit liver microsomesBiochemical and Biophysical Research Communications, 1979
- Amino-terminal sequence of phenobarbital-inducible cytochrome P-450 from rabbit liver microsomes: Similarity to hydrophobic amino-terminal segments of preproteinsBiochemical and Biophysical Research Communications, 1977
- Highly purified detergent-solubilized NADPH-cytochrome P-450 reductase from phenobarbital-induced rat liver microsomesBiochemical and Biophysical Research Communications, 1974
- Identification of the ω-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein requiring phospholipid for catalytic activityBiochemical and Biophysical Research Communications, 1974
- Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds and endogenous substrates: I. Determination of substrate specificity by the cytochrome P-450 and P-448 fractionsBiochemical and Biophysical Research Communications, 1971
- Hydroxylation of benzphetamine and other drugs by a solubilized form of cytochrome P-450 from liver microsomes: Lipid requirement for drug demethylationBiochemical and Biophysical Research Communications, 1969