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An Iterative Module in the Azalomycin F Polyketide Synthase Contains a Switchable Enoylreductase Domain.

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cam.issuedOnline2017-04-18
dc.contributor.authorXu, Wei
dc.contributor.authorZhai, Guifa
dc.contributor.authorLiu, Yuanzhen
dc.contributor.authorLi, Yuan
dc.contributor.authorShi, Yanrong
dc.contributor.authorHong, Kui
dc.contributor.authorHong, Hui
dc.contributor.authorLeadlay, Peter F
dc.contributor.authorDeng, Zixin
dc.contributor.authorSun, Yuhui
dc.contributor.orcidLeadlay, Peter [0000-0002-3247-509X]
dc.date.accessioned2018-09-05T12:47:46Z
dc.date.available2018-09-05T12:47:46Z
dc.date.issued2017-05-08
dc.description.abstractDetailed analysis of the modular Type I polyketide synthase (PKS) involved in the biosynthesis of the marginolactone azalomycin F in mangrove Streptomyces sp. 211726 has shown that only nineteen extension modules are required to accomplish twenty cycles of polyketide chain elongation. Analysis of the products of a PKS mutant specifically inactivated in the dehydratase domain of extension-module 1 showed that this module catalyzes two successive elongations with different outcomes. Strikingly, the enoylreductase domain of this module can apparently be "toggled" off and on : it functions in only the second of these two cycles. This novel mechanism expands our understanding of PKS assembly-line catalysis and may explain examples of apparent non-colinearity in other modular PKS systems.
dc.format.mediumPrint-Electronic
dc.identifier.doi10.17863/CAM.26920
dc.identifier.eissn1521-3773
dc.identifier.issn1433-7851
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/279548
dc.languageeng
dc.language.isoeng
dc.publisherWiley
dc.publisher.urlhttp://dx.doi.org/10.1002/anie.201701220
dc.rightsAttribution-NonCommercial 4.0 International (CC BY-NC 4.0)
dc.subjectantibiotics
dc.subjectbiosynthesis
dc.subjectenoylreductases
dc.subjectiteration modules
dc.subjectmacrocyclic polyketides
dc.subjectMacrolides
dc.subjectMolecular Conformation
dc.subjectMutation
dc.subjectOxidoreductases
dc.subjectPolyketide Synthases
dc.titleAn Iterative Module in the Azalomycin F Polyketide Synthase Contains a Switchable Enoylreductase Domain.
dc.typeArticle
prism.endingPage5506
prism.issueIdentifier20
prism.publicationDate2017
prism.publicationNameAngew Chem Int Ed Engl
prism.startingPage5503
prism.volume56
pubs.funder-project-idBiotechnology and Biological Sciences Research Council (BB/I002413/1)
rioxxterms.licenseref.startdate2017-05
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.typeJournal Article/Review
rioxxterms.versionVoR
rioxxterms.versionofrecord10.1002/anie.201701220

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