dc.creatorZhou, Yongjun
dc.creatorPrediger, Patrícia
dc.creatorDias, Luiz Carlos
dc.creatorMurphy, Annabel C
dc.creatorLeadlay, Peter F
dc.date2015-Apr
dc.date2016-05-23T19:41:14Z
dc.date2016-05-23T19:41:14Z
dc.date.accessioned2018-03-29T01:28:44Z
dc.date.available2018-03-29T01:28:44Z
dc.identifierAngewandte Chemie (weinheim An Der Bergstrasse, Germany). v. 127, n. 17, p. 5321-5324, 2015-Apr.
dc.identifier0044-8249
dc.identifier10.1002/ange.201500401
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/?term=26300568
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/235488
dc.identifier26300568
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1303731
dc.descriptionElaiophylin is an unusual C2-symmetric antibiotic macrodiolide produced on a bacterial modular polyketide synthase assembly line. To probe the mechanism and selectivity of diolide formation, we sought to reconstitute ring formation in vitro by using a non-natural substrate. Incubation of recombinant elaiophylin thioesterase/cyclase with a synthetic pentaketide analogue of the presumed monomeric polyketide precursor of elaiophylin, specifically its N-acetylcysteamine thioester, produced a novel 16-membered C2-symmetric macrodiolide. A linear dimeric thioester is an intermediate in ring formation, which indicates iterative use of the thioesterase active site in ligation and subsequent cyclization. Furthermore, the elaiophylin thioesterase acts on a mixture of pentaketide and tetraketide thioesters to give both the symmetric decaketide diolide and the novel asymmetric hybrid nonaketide diolide. Such thioesterases have potential as tools for the in vitro construction of novel diolides.
dc.description127
dc.description5321-5324
dc.languageeng
dc.relationAngewandte Chemie (weinheim An Der Bergstrasse, Germany)
dc.relationAngew Chem Weinheim Bergstr Ger
dc.rightsembargo
dc.sourcePubMed
dc.subjectBiosynthese
dc.subjectDiolide
dc.subjectElaiophylin
dc.subjectPolyketid-synthase
dc.subjectThioesterase
dc.titleMacrodiolide Formation By The Thioesterase Of A Modular Polyketide Synthase.
dc.typeArtículos de revistas


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