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Biosci Biotechnol Biochem. 2006 Jan;70(1):307-11.

Hydroxylation of testosterone by bacterial cytochromes P450 using the Escherichia coli expression system.

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1
Bioresource Laboratories, Mercian Corp, Japan. agematsu-h@mercian.co.jp

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.

PMID:
16428858
DOI:
10.1271/bbb.70.307
[Indexed for MEDLINE]
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