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

Biosci Biotechnol Biochem. 2006 Jan;70(1):307-11. doi: 10.1271/bbb.70.307.


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.

MeSH terms

  • Chromatography, High Pressure Liquid
  • Cytochrome P-450 Enzyme System / genetics
  • Cytochrome P-450 Enzyme System / metabolism*
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics*
  • Gene Expression Regulation, Bacterial / genetics*
  • Humans
  • Hydroxylation
  • Molecular Structure
  • Testosterone / chemistry*
  • Testosterone / metabolism*


  • Testosterone
  • Cytochrome P-450 Enzyme System