title: Hydroxylation of testosterone by bacterial cytochromes P450 using the Escherichia coli expression system.
abstract: Two hundred thirteen cytochrome P450 (P450) genes were collected from bacteria and expressed based on an Escherichia coli expression system to test their hydroxylation ability to testosterone. Twenty-four P450s stereoselectively monohydroxylated testosterone at the 2alpha-, 2beta-, 6beta-, 7beta-, 11beta-, 12beta-, 15beta-, 16alpha-, and 17-positions (17-hydroxylation yields 17-ketoproduct). The hydroxylation site usage of the P450s is not the same as that of human P450s, while the 2alpha-, 2beta-, 6beta-, 11beta-, 15beta-, 16alpha-, and 17-hydroxylation are reactions common to both human and bacterial P450s. Most of the testosterone hydroxylation catalyzed by bacterial P450s is on the beta face.
authors.affiliation: Bioresource Laboratories, Mercian Corp, Japan. agematsu-h@mercian.co.jp
authors.forename: Hitosi
authors.initials: H
authors.lastname: Agematu
authors.forename: Naoki
authors.initials: N
authors.lastname: Matsumoto
authors.forename: Yoshikazu
authors.initials: Y
authors.lastname: Fujii
authors.forename: Hiroki
authors.initials: H
authors.lastname: Kabumoto
authors.forename: Satoru
authors.initials: S
authors.lastname: Doi
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Machida
authors.forename: Jun
authors.initials: J
authors.lastname: Ishikawa
authors.forename: Akira
authors.initials: A
authors.lastname: Arisawa
mesh_terms: D002851:Chromatography, High Pressure Liquid; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial / Q000235:genetics*; D006801:Humans; D006900:Hydroxylation; D015394:Molecular Structure; D013739:Testosterone / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D013739:Testosterone; D003577:Cytochrome P-450 Enzyme System