Journal
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 76, Issue 6, Pages 1975-1980Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.03000-09
Keywords
-
Categories
Funding
- National Institutes of Health [R01GM69970, P30ES00267]
- Leverhulme Trust
- Royal Society
- Biotechnology and Biological Sciences Research Council [BB/E019242/1] Funding Source: researchfish
- BBSRC [BB/E019242/1] Funding Source: UKRI
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available