Characterisation of CYP102A25 from B. marmarensis and CYP102A26 from P. halophilus: P450 homologues of BM3 with preference towards hydroxylation of medium chain fatty acids.
- Joanne L Porter,
- Jack Manning,
- Selina Sabatini,
- Michele Tavanti,
- Nicholas J Turner,
- Sabine L Flitsch
Chembiochem 2017 Dec 8. Epub 2017 Dec 8.
University of Manchester, Manchester Institute of Biotechnology, 131 Princess St, M1 7DN, Manchester, UNITED KINGDOM.
Cytochrome P450 monooxgenases are highly desired biocatalysts due to their ability to catalyse a wide variety of chemically challenging C-H activation reactions. The CYP102A subfamily of enzymes are natural catalytically self-sufficient proteins consisting of a haem and FMN-FAD reductase domain fused in a single component system. They catalyse the oxygenation of saturated and unsaturated fatty acids to produce primarily ω-1, ω-2 and ω-3 hydroxy acids. Read More