title: P450(BM3) on steroids: the Swiss Army knife P450 enzyme just gets better.
abstract: The catalytic regio- and stereoselective oxidation of aliphatic C-H bonds by using atmospheric dioxygen as the oxidant is a highly desirable reaction. Reetz and co-workers have recently reported the development of P450(BM3) mutants that oxidise testosterone with greatly increased turnover activity, total stereoselectivity and >95 % regioselectivity.
authors: Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, Oxford OX1 3QR, UK. luet.wong@chem.ox.ac.uk
authors: Luet-Lok
authors: LL
authors: Wong
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D055162:Biocatalysis; D020134:Catalytic Domain; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010084:Oxidation-Reduction; D017433:Protein Structure, Secondary; D013237:Stereoisomerism; D013256:Steroids / Q000737:chemistry / Q000378:metabolism*; D013739:Testosterone / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D013256:Steroids; D013739:Testosterone; D003577:Cytochrome P-450 Enzyme System; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases