Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
dc.contributor.author | Moretto, L | |
dc.contributor.author | Vance, S | |
dc.contributor.author | Heames, B | |
dc.contributor.author | Broadhurst, RW | |
dc.date.accessioned | 2018-09-08T06:32:03Z | |
dc.date.available | 2018-09-08T06:32:03Z | |
dc.identifier.uri | https://www.repository.cam.ac.uk/handle/1810/279838 | |
dc.description.abstract | Interaction 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.sponsorship | The 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.publisher | Royal Society of Chemistry | |
dc.rights | Attribution 4.0 International (CC BY 4.0) | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.title | Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates | |
dc.type | Article | |
prism.endingPage | 11460 | |
prism.publicationName | Chemical Communications | |
prism.startingPage | 11457 | |
prism.volume | 53 | |
dc.identifier.doi | 10.17863/CAM.27206 | |
dcterms.dateAccepted | 2017-06-29 | |
rioxxterms.versionofrecord | 10.1039/c7cc04625a | |
rioxxterms.licenseref.uri | http://creativecommons.org/licenses/by/4.0/ | |
rioxxterms.licenseref.startdate | 2017-06-29 | |
dc.contributor.orcid | Broadhurst, Bill [0000-0002-0264-4593] | |
rioxxterms.type | Journal Article/Review | |
pubs.funder-project-id | Wellcome Trust (094252/Z/10/Z) | |
cam.issuedOnline | 2017-10-05 |
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