Hydroxylation of testosterone by bacterial cytochromes P450 using the Escherichia coli expression system.
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.
Agematu
Hitosi
H
Bioresource Laboratories, Mercian Corp, Japan. agematsu-h@mercian.co.jp
Matsumoto
Naoki
N
Fujii
Yoshikazu
Y
Kabumoto
Hiroki
H
Doi
Satoru
S
Machida
Kazuhiro
K
Ishikawa
Jun
J
Arisawa
Akira
A
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*
D013739:Testosterone; D003577:Cytochrome P-450 Enzyme System