Hydroxylation of Testosterone by Bacterial Cytochromes P450 Using the<i>Escherichia coli</i>Expression System

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  • Hydroxylation of Testosterone by Bacterial Cytochromes P450 Using the Escherichia coli Expression System
  • Hydroxylation of testosterone by bacterial cytochrome P450 using the Escherichia coli expression system

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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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