Streptomyces coelicolor A3(2) CYP102 protein, a novel fatty acid hydroxylase encoded as a heme domain without an N-terminal redox partner.

@article{Lamb2010StreptomycesCA,
  title={Streptomyces coelicolor A3(2) CYP102 protein, a novel fatty acid hydroxylase encoded as a heme domain without an N-terminal redox partner.},
  author={David Christopher Lamb and Li Lei and Bin Zhao and Hang Yuan and Colin J Jackson and Andrew Graham Samuel Warrilow and Tove Skaug and Paul J Dyson and Eric Dawson and Steven L Kelly and David L. Hachey and Michael R. Waterman},
  journal={Applied and environmental microbiology},
  year={2010},
  volume={76 6},
  pages={1975-80}
}
The gene from Streptomyces coelicolor A3(2) encoding CYP102B1, a recently discovered CYP102 subfamily which exists solely as a single P450 heme domain, has been cloned, expressed in Escherichia coli, purified, characterized, and compared to its fusion protein family members. Purified reconstitution metabolism experiments with spinach ferredoxin, ferredoxin reductase, and NADPH revealed differences in the regio- and stereoselective metabolism of arachidonic acid compared to that of CYP102A1… CONTINUE READING