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

被引：116

作者：

Agematu, H

Matsumoto, N

Fujii, Y

Kabumoto, H

Doi, S

Machida, K

Ishikawa, J

Arisawa, A

机构：

[1] Mercian Corp, Bioresource Labs, Shizuoka 4380078, Japan

[2] Natl Inst Infect Dis, Tokyo 1628640, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2006年 / 70卷 / 01期

关键词：

cytochrorne P450; testosterone; hydroxylation; bioconversion;

D O I：

10.1271/bbb.70.307

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 2 alpha-, 2 beta-, 6 beta-, 7 beta-, 11 beta-, 12 beta-, 15 beta-, 16 beta-, 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 2 alpha-, 2 beta-, 6 beta-, 11 beta-, 15 beta-, 16 alpha-, 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.

引用

页码：307 / 311

页数：5

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