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dc.contributor.authorPaulus, Constanze
dc.contributor.authorRebets, Yuriy
dc.contributor.authorZapp, Josef
dc.contributor.authorRückert, Christian
dc.contributor.authorKalinowski, Jörn
dc.contributor.authorLuzhetskyy, Andriy N
dc.date.accessioned2018-10-23T09:11:11Z
dc.date.available2018-10-23T09:11:11Z
dc.date.issued2018-01-01
dc.identifier.issn1664-302X
dc.identifier.pmid30186270
dc.identifier.doi10.3389/fmicb.2018.01959
dc.identifier.urihttp://hdl.handle.net/10033/621522
dc.description.abstracthe environment of Lake Baikal is a well-known source of microbial diversity. The strain Streptomyces sp. IB2014/011-12, isolated from samples collected at Lake Baikal, was found to exhibit potent activity against Gram-positive bacteria. Here, we report isolation and characterization of linear polyketide alpiniamide A (1) and its new derivatives B–D (2–5). The structures of alpiniamides A–D were established and their relative configuration was determined by combination of partial Murata’s method and ROESY experiment. The absolute configuration of alpiniamide A was established through Mosher’s method. The gene cluster, responsible for the biosynthesis of alpiniamides (alp) has been identified by genome mining and gene deletion experiments. The successful expression of the cloned alp gene cluster in a heterologous host supports these findings. Analysis of the architecture of the alp gene cluster and the feeding of labeled precursors elucidated the alpiniamide biosynthetic pathway. The biosynthesis of alpiniamides is an example of a rather simple polyketide assembly line generating unusual chemical diversity through the combination of domain/module skipping and double bond migration events.en_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.subjectNRPS-trans-AT-polyketide synthaseen_US
dc.subjectStreptomycesen_US
dc.subjectbioactivityen_US
dc.subjectsecondary metabolitesen_US
dc.subjectstereochemistryen_US
dc.titleNew Alpiniamides From sp. IB2014/011-12 Assembled by an Unusual Hybrid Non-ribosomal Peptide Synthetase -AT Polyketide Synthase Enzyme.en_US
dc.typeArticleen_US
dc.contributor.departmentHIPS, Helmholtz-Institut füt Pharmazeutische Forschung Saarland, Universitätscampus E8.1 66123 Saarbrücken, Germany.en_US
refterms.dateFOA2018-10-23T09:11:12Z
dc.source.journaltitleFrontiers in microbiology


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