Journal
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 67, Issue 5, Pages 2136-2138Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.67.5.2136-2138.2001
Keywords
-
Categories
Ask authors/readers for more resources
CYP105D1, a cytochrome P450 from Streptomyces griseus, was appended at its amino terminus to the secretory signal of Escherichia coli alkaline phosphatase and placed under the transcriptional control of the native phoA promoter. Heterologous expression in E. coli phosphate-limited medium resulted in abundant synthesis of recombinant CYP105D1 that was translocated across the bacterial inner membrane and processed to yield authentic, heme-incorporated P450 within the periplasmic space. Cell extract and whole-cell activity studies shun;ed that the periplasmically located CYP105D1 competently catalyzed NADH-dependent oxidation of the xenobiotic compounds benzo[a]pyrene and erythromycin, further revealing the presence in the E. coli periplasm of endogenous functional redox partners, This system offers substantial advantages for the application of P450 enzymes to whole-cell biotransformation strategies, H here the ability of cells to take up substrates or discard products may be limited.
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