期刊
CHEMISTRY & BIOLOGY
卷 12, 期 7, 页码 825-833出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2005.05.015
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资金
- Biotechnology and Biological Sciences Research Council [BBS/B/07071] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [BBS/B/07071] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [GR/S78124/01] Funding Source: researchfish
Mupirocin, a polyketide-derived antibiotic from Pseudomonas fluorescens NCIMB10586, is a mixture of pseudomonic acids (PA) that target isoleucyl-tRNA synthase. The mup gene cluster encodes both type I polyketide synthases and monofunctional enzymes that should play a role during the conversion of the product of the polyketide synthase into the active antibiotic (tailoring). By in-frame deletion analysis of selected tailoring open-reading frames we show that mupQ, mupS, mupT, and mupW are essential for mupirocin production, whereas mupO, mupU, mupV, and macpE are essential for production of PA-A but not PA-B. Therefore, PA-B is not simply produced by hydroxylation of PA-A but is either a precursor of PA-A or a shunt product. In the mupW mutant, a new metabolite lacking the tetrahydropyran ring is produced, implicating mupW in oxidation of the 16-methyl group.
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