Hydroxylation of Testosterone by Bacterial Cytochromes P450 Using the Escherichia coli Expression System

Hitosi AGEMATU; Naoki MATSUMOTO; Yoshikazu FUJII; Hiroki KABUMOTO; Satoru DOI; Kazuhiro MACHIDA; Jun ISHIKAWA; Akira ARISAWA

doi:10.1271/bbb.70.307

Biochemistry & Molecular Biology Communications

Hydroxylation of Testosterone by Bacterial Cytochromes P450 Using the Escherichia coli Expression System

Hitosi AGEMATU, Naoki MATSUMOTO, Yoshikazu FUJII, Hiroki KABUMOTO, Satoru DOI, Kazuhiro MACHIDA, Jun ISHIKAWA, Akira ARISAWA

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Keywords: cytochrome P450, testosterone, hydroxylation, bioconversion

JOURNAL FREE ACCESS

2006 Volume 70 Issue 1 Pages 307-311

DOI https://doi.org/10.1271/bbb.70.307

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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 2α-, 2β-, 6β-, 7β-, 11β-, 12β-, 15β-, 16α-, 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 2α-, 2β-, 6β-, 11β-, 15β-, 16α-, and 17-hydroxylation are reactions common to both human and bacterial P450s. Most of the testosterone hydroxylation catalyzed by bacterial P450s is on the β face.

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