title: Analysis of the catalytic specificity of cytochrome P450 enzymes through site-directed mutagenesis.
abstract: The way in which structural diversity encodes the capacity of individual P450 enzymes to metabolize multiple, structurally distinct substrates remains largely unknown. The tools of molecular biology provide a means of identifying amino acid residues among closely related P450s that are determinants of their distinct catalytic properties. Work in our laboratory has identified two substrate specificity-determining segments of the amino acid sequences of subfamily 2C P450s. A pattern has emerged from this work, and that of others, which suggests a model for the structural basis of P450 catalytic diversity.
authors.affiliation: Scripps Research Institute, Division of Biochemistry, La Jolla, California 92037.
authors.forename: E F
authors.initials: EF
authors.lastname: Johnson
authors.forename: T
authors.initials: T
authors.lastname: Kronbach
authors.forename: M H
authors.initials: MH
authors.lastname: Hsu
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics* / Q000378:metabolism*; D014644:Genetic Variation; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D012326:RNA Splicing; D012689:Sequence Homology, Nucleic Acid; D013255:Steroid 21-Hydroxylase / Q000235:genetics / Q000378:metabolism
chemical_list: D003577:Cytochrome P-450 Enzyme System; D013255:Steroid 21-Hydroxylase