Hydroxylation of Testosterone by Bacterial Cytochromes P450 Using the Escherichia coli Expression System
Two hundred thirteen cytochrome P450 (P450) genes were collected from bacteria and expressed based on an <I>Escherichia coli</I> 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.
- Bioscience, biotechnology, and biochemistry
Bioscience, biotechnology, and biochemistry 70(1), 307-311, 2006-01-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry