Selective steroid oxyfunctionalisation by CYP154C5, a bacterial cytochrome P450

@inproceedings{Bracco2013SelectiveSO,
  title={Selective steroid oxyfunctionalisation by CYP154C5, a bacterial cytochrome P450},
  author={Paula Bracco and Dick B. Janssen and Anett Schallmey},
  booktitle={Microbial cell factories},
  year={2013}
}
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 16… CONTINUE READING
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Steroid hydroxylation: microbial steroid biotransformations using cytochrome P450 enzymes

  • M Bureik, R Bernhardt
  • In Modern Biooxidation. Edited by Schmid RD…
  • 2013
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