Michael Waterman
Faculty Member
Last active: 2/12/2015

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

Lamb DC, Lei L, Zhao B, Yuan H, Jackson CJ, Warrilow AG, Skaug T, Dyson PJ, Dawson ES, Kelly SL, Hachey DL, Waterman MR
Appl Environ Microbiol. 2010 76 (6): 1975-80

PMID: 20097805 · PMCID: PMC2838009 · DOI:10.1128/AEM.03000-09

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, exclusively producing 11,12-epoxyeicosa-5,8,14-trienoic acid in addition to the shared metabolites 18-hydroxy arachidonic acid and 14,15-epoxyeicosa-5,8,11-trienoic acid. Consequently, in order to elucidate the physiological function of CYP102B1, transposon mutagenesis was used to generate an S. coelicolor A3(2) strain lacking CYP102B1 activity and the phenotype was assessed.

MeSH Terms (14)

8,11,14-Eicosatrienoic Acid Arachidonic Acid Cloning, Molecular Cytochrome P-450 Enzyme System DNA Transposable Elements Escherichia coli Ferredoxin-NADP Reductase Ferredoxins Gene Expression Mixed Function Oxygenases Mutagenesis, Insertional NADP Streptomyces coelicolor Substrate Specificity

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