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dc.contributor.authorMoretto, Len
dc.contributor.authorVance, Sen
dc.contributor.authorHeames, Ben
dc.contributor.authorBroadhurst, Billen
dc.date.accessioned2018-09-08T06:32:03Z
dc.date.available2018-09-08T06:32:03Z
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/279838
dc.description.abstractInteraction studies using fragments excised from the modular mycolactone polyketide synthase show that ketoreductase domains possess a generic binding site for acyl carrier protein domains and provide evidence that the pendant 5′-phosphopantetheine prosthetic group plays a key role in delivering acyl substrates to the active site in the correct orientation.
dc.description.sponsorshipThe authors would like to thank the Wellcome Trust (grant number 094252/Z/10/Z) for funding this research. LM was supported by an EPSRC PhD studentship.
dc.publisherRoyal Society of Chemistry
dc.rightsAttribution 4.0 International (CC BY 4.0)
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleDissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substratesen
dc.typeArticle
prism.endingPage11460
prism.publicationNameChemical Communicationsen
prism.startingPage11457
prism.volume53en
dc.identifier.doi10.17863/CAM.27206
dcterms.dateAccepted2017-06-29en
rioxxterms.versionofrecord10.1039/c7cc04625aen
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/en
rioxxterms.licenseref.startdate2017-06-29en
dc.contributor.orcidBroadhurst, Bill [0000-0002-0264-4593]
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idWellcome Trust (094252/Z/10/Z)
cam.issuedOnline2017-10-05en


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Attribution 4.0 International (CC BY 4.0)
Except where otherwise noted, this item's licence is described as Attribution 4.0 International (CC BY 4.0)