title: Regioselective hydroxylation of 17β-estradiol by mutants of CYP102A1 from Bacillus megaterium.
abstract: A large set of mutants of CYP102A1 from Bacillus megaterium have human cytochrome P450-like activities and the ability to metabolize a number of marketed drugs and steroids. Here, we tested whether the CYP102A1 mutants could be used to produce hydroxylated human metabolites of 17β-estradiol (E2). A set of the mutants, which were generated by site-directed and random mutagenesis, was used to produce hydroxylated human metabolites of E2 in this study. Some of the tested mutants could regioselectively generate 2-OH E2 as a major metabolite but not other hydroxylated products. These results suggest that CYP102A1 mutants would be useful for the bioconversion of steroid hormones to hydroxylated products, which can be used for industrial applications.
authors.affiliation: School of Biological Sciences and Technology, Chonnam National University, Gwangju, 500-757, Republic of Korea.
authors.forename: Gun Su
authors.initials: GS
authors.lastname: Cha
authors.forename: Sang Hoon
authors.initials: SH
authors.lastname: Ryu
authors.forename: Taeho
authors.initials: T
authors.lastname: Ahn
authors.forename: Chul-Ho
authors.initials: CH
authors.lastname: Yun
mesh_terms: D001410:Bacillus megaterium / Q000201:enzymology* / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001711:Biotransformation; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics / Q000378:metabolism*; D004958:Estradiol / Q000378:metabolism*; D006900:Hydroxylation; D016296:Mutagenesis; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism*; D009251:NADPH-Ferrihemoprotein Reductase / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D050505:Mutant Proteins; D004958:Estradiol; D003577:Cytochrome P-450 Enzyme System; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases