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dc.contributor.authorWang, Yuanyou
dc.contributor.authorSchnell, Bastien
dc.contributor.authorBaumann, Sascha
dc.contributor.authorMüller, Rolf
dc.contributor.authorBegley, Tadhg P
dc.date.accessioned2018-10-30T14:22:41Z
dc.date.available2018-10-30T14:22:41Z
dc.date.issued2017-02-08
dc.identifier.issn1520-5126
dc.identifier.pmid28040895
dc.identifier.doi10.1021/jacs.6b10901
dc.identifier.urihttp://hdl.handle.net/10033/621524
dc.description.abstractThe biosynthesis of branched alkoxy groups, such as the unique t-butyl group found in a variety of natural products, is still poorly understood. Recently, cystobactamids were isolated and identified from Cystobacter sp as novel antibacterials. These metabolites contain an isopropyl group proposed to be formed using CysS, a cobalamin-dependent radical S-adenosylmethionine (SAM) methyltransferase. Here, we reconstitute the CysS-catalyzed reaction, on p-aminobenzoate thioester substrates, and demonstrate that it not only catalyzes sequential methylations of a methyl group to form ethyl and isopropyl groups but remarkably also sec-butyl and t-butyl groups. To our knowledge, this is the first in vitro reconstitution of a cobalamin-dependent radical SAM enzyme catalyzing the conversion of a methyl group to a t-butyl group.en_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.titleBiosynthesis of Branched Alkoxy Groups: Iterative Methyl Group Alkylation by a Cobalamin-Dependent Radical SAM Enzyme.en_US
dc.typeArticleen_US
dc.contributor.departmentHIPS, Helmholtz-Institut füt Pharmazeutische Forschung Saarland, Universitätscampus E8.1 66123 Saarbrücken, Germany.en_US
refterms.dateFOA2018-10-30T14:22:41Z
dc.source.journaltitleJournal of the American Chemical Society


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