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Abstract
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.
Original language | English |
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Pages (from-to) | 825-833 |
Number of pages | 9 |
Journal | Chemistry & Biology |
Volume | 12 |
Issue number | 7 |
DOIs | |
Publication status | Published - 1 Jul 2005 |
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Dive into the research topics of 'Shift to pseudomonic acid B production in P-fluorescens NCIMB10586 by mutation of Mupirocin tailoring genes mupO, mupV, and macpE'. Together they form a unique fingerprint.Projects
- 1 Finished
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Biosynthesis of the Polyketide Antibiotic Mupirocin by Pseudomonas Fluorescens
Biotechnology & Biological Sciences Research Council
14/05/04 → 13/05/07
Project: Research Councils