期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 70, 期 1, 页码 307-311出版社
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.70.307
关键词
cytochrorne P450; testosterone; hydroxylation; bioconversion
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据