Journal of Biological Chemistry · 1991 · 603 citations · 58 references
Life SciencesBiochemistryEnzyme MechanismEnzymologyProtein BiochemistryCytochrome P450 EnzymesEnzyme CharacterizationEnzyme FunctionEnzyme SpecificityEnzyme-substrate RecognitionSubstrate SpecificityCatalytic SpecificityConserved Region AnalysisCytochrome P450 CatalysisCytochrome P450 Enzyme ActivityCytochrome P450 IsoenzymesCytochrome P450 Reaction MechanismsCytochrome P450 Structure-function RelationshipsCytochrome P450 Substrate Specificity
complex has a characteristic absorption maximum (Soret band) near 450 nm due to axial ligation with a cysteine thiolate of the protein (with or without substrate present). This cysteine residue is present in a relatively well conserved region, -80% into the protein from the N terminus. Collectively there are thousands of potential substrates for the P-450s; each of the P-450s may have a rather strict limitation of catalytic specificity
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Muneaki Imai, H. Shimada, Yoshihito Watanabe et al. · Proceedings of the National Academy of Sciences · 1989 · 374 citations · Full text