title: Biotransformation of (-)-camphor by Salmonella typhimurium OY1002/2A6 expressing human CYP2A6 and NADPH-P450 reductase.
abstract: In a previous in vitro study, (-)-camphor (1) was examined by incubation with human liver microsomes, and the oxidative metabolites thus formed were analyzed using gas chromatography-mass spectrometry. However, thus far, no large-scale biotransformation using recombinant human P450 has been performed. Here, the biotransformation of compound 1 has been investigated by using Salmonella typhimurium OY1002/2A6 expressing human CYP2A6 and human NADPH-P450 reductase as a biocatalyst. Compound 1 (400 mg) was converted to (1S,5S)-(-)-5-exo-hydroxycamphor (2) (30.4 mg) and (1S,7S)-(-)-8-hydroxycamphor (3) (2.4 mg) by S. typhimurium OY1002/2A6. This is the first report to show that large quantities of metabolites 2 and 3 can be produced by S. typhimurium OY1002/2A6 expressing human CYP2A6 and NADPH-P450 reductase.
authors.affiliation: Department of Applied Chemistry, Faculty of Science and Engineering, Kinki University, Osaka, Japan. miyazawa@apch.kindai.ac.jp
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Nakahashi
authors.forename: Mitsuo
authors.initials: M
authors.lastname: Miyazawa
mesh_terms: D001189:Aryl Hydrocarbon Hydroxylases / Q000235:genetics / Q000378:metabolism*; D055162:Biocatalysis; D001711:Biotransformation; D002164:Camphor / Q000737:chemistry / Q000378:metabolism*; D065637:Cytochrome P-450 CYP2A6; D006801:Humans; D015394:Molecular Structure; D009251:NADPH-Ferrihemoprotein Reductase / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012486:Salmonella typhimurium / Q000235:genetics / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; D002164:Camphor; D001189:Aryl Hydrocarbon Hydroxylases; C585710:CYP2A6 protein, human; D065637:Cytochrome P-450 CYP2A6; D009251:NADPH-Ferrihemoprotein Reductase