Journal
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 79, Issue 19, Pages 6156-6159Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.02197-13
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Funding
- Science Foundation Ireland [09/RFP/GEN2132]
- BBSRC [BB/D017270/1] Funding Source: UKRI
- Science Foundation Ireland (SFI) [09/RFP/GEN2132] Funding Source: Science Foundation Ireland (SFI)
- Biotechnology and Biological Sciences Research Council [BB/D017270/1] Funding Source: researchfish
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Recent work has uncovered genes for two glycosyltransferases that are thought to catalyze mannosylation of mycosaminyl sugars of polyene macrolides. These two genes are nypY from Pseudonocardia sp. strain P1 and pegA from Actinoplanes caeruleus. Here we analyze these genes by heterologous expression in various strains of Streptomyces nodosus, producer of amphotericins, and in Streptomyces albidoflavus, which produces candicidins. The NypY glycosyltransferase converted amphotericins A and B and 7-oxo-amphotericin B to disaccharide-modified forms in vivo. The enzyme did not act on amphotericin analogs lacking exocyclic carboxyl or mycosamine amino groups. Both NypY and PegA acted on candicidins. This work confirms the functions of these glycosyltransferases and provides insights into their acceptor substrate tolerance. Disaccharide-modified polyenes may have potential as less toxic antibiotics.
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