Molecular Control of Polyene Macrolide Biosynthesis
نویسندگان
چکیده
منابع مشابه
The polyene macrolide antibiotics.
The mode of action of the polyene antibiotics is reviewed together with the effect of genetic and environmental factors on sensitive organisms. The future prospects of polyenes in the treatment of systemic mycoses are considered.
متن کاملN-glycosyl derivatives of polyene macrolide antibiotics.
Sir: The polyene macrolides are known as potent antifungal agents. However their use in therapy is limited by considerable toxicity and very poor water solubility. Many efforts had been taken to obvert these undesirable properties1-5). We report now a new group of derivatives of polyene macrolides exhibiting improved solubility in water and organic solvents and retaining the biological activity...
متن کاملRedesign of polyene macrolide glycosylation: engineered biosynthesis of 19-(O)-perosaminyl-amphoteronolide B.
Most polyene macrolide antibiotics are glycosylated with mycosamine (3,6-dideoxy-3-aminomannose). In the amphotericin B producer, Streptomyces nodosus, mycosamine biosynthesis begins with AmphDIII-catalyzed conversion of GDP-mannose to GDP-4-keto-6-deoxymannose. This is converted to GDP-3-keto-6-deoxymannose, which is transaminated to GDP-mycosamine by the AmphDII protein. The glycosyltransfera...
متن کاملTrichomycin B, a polyene macrolide from Streptomyces.
Two polyene macrolide, trichomycins A and B, were compared by physico-chemical and microbiological methods. The two antibiotics were found to have the same molecular formula, C58H84N2O18 (MW 1,096), by elemental analysis and FAB-MS. However, 1H and 13C NMR spectrometry studies indicated that the hydroxyl at C-5 of trichomycin A located on C-9 in trichomycin B. Trichomycin B possessed lower acti...
متن کاملHierarchical Control on Polyene Macrolide Biosynthesis: PimR Modulates Pimaricin Production via the PAS-LuxR Transcriptional Activator PimM
Control of polyene macrolide production in Streptomyces natalensis is mediated by the transcriptional activator PimR. This regulator combines an N-terminal domain corresponding to the Streptomyces antibiotic regulatory protein (SARP) family of transcriptional activators with a C-terminal half homologous to guanylate cyclases and large ATP-binding regulators of the LuxR family. The PimR SARP dom...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2011
ISSN: 0021-9258
DOI: 10.1074/jbc.m110.182428