title: Mutations at the distal and proximal sites of cytochrome P-450d changed regio-specificity of acetanilide hydroxylations.
abstract: Regio-specificities of acetanilide hydroxylations were studied for 11 distal, 9 proximal and 3 aromatic mutants of cytochrome P-450d. Ratios of turnover numbers among these products were remarkably changed depending on the mutants. For example, the ratio of turnover number, para:ortho:meta = 7:0.1:0.3 for the wild type changed to 11:4:3 for a distal mutant, Thr322Ala, or to 13:13:1 for a proximal mutant, Arg455Gly. It was suggested that regio-specificities of microsomal P-450 enzymes are controlled cooperatively by the whole structure of the protein molecules which influences the tertiary structure of the distal environment.
authors.affiliation: Chemical Research Institute of Non-Aqueous Solutions, Tohoku University, Sendai, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Furuya
authors.forename: T
authors.initials: T
authors.lastname: Shimizu
authors.forename: M
authors.initials: M
authors.lastname: Hatano
authors.forename: Y
authors.initials: Y
authors.lastname: Fujii-Kuriyama
mesh_terms: D000083:Acetanilides; D000596:Amino Acids / Q000235:genetics; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics*; D006900:Hydroxylation; D051379:Mice; D009154:Mutation; D051381:Rats
chemical_list: D000083:Acetanilides; D000596:Amino Acids; D003577:Cytochrome P-450 Enzyme System