Selective steroid oxyfunctionalisation by CYP154C5, a bacterial cytochrome P450.

ABSTRACT:

Background

Cytochrome P450 monooxygenases--able to regio- and stereoselectively hydroxylate non-activated carbon atoms--are important enzymes for the synthesis of valuable intermediates in the production of steroid hormones in the pharmaceutical industry. However, up to now only a few bacterial enzymes able to hydroxylate steroids have been reported. CYP154C5 from Nocardia farcinica IFM 10152, a bacterial P450 monooxygenase, was previously shown to convert testosterone to 16α-hydroxytestosterone. Since the hydroxylation at 16α-position is of special interest for the pharmaceutical industry, we have studied this enzyme in more detail to investigate its activity and selectivity in bioconversions of further steroids.

Results

CYP154C5 was coexpressed in Escherichia coli together

SUBMITTER: Bracco P 

PROVIDER: S-EPMC4015549 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature