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dc.contributor.authorGao, Sisi
dc.contributor.authorGe, Ying
dc.contributor.authorBent, Andrew F.
dc.contributor.authorSchwarz-Linek, Ulrich
dc.contributor.authorNaismith, James H.
dc.date.accessioned2019-09-11T23:37:30Z
dc.date.available2019-09-11T23:37:30Z
dc.date.issued2018-10-16
dc.identifier.citationGao , S , Ge , Y , Bent , A F , Schwarz-Linek , U & Naismith , J H 2018 , ' Oxidation of the cyanobactin precursor peptide is independent of the leader peptide and operates in a defined order ' , Biochemistry , vol. 57 , no. 41 , pp. 5996-6002 . https://doi.org/10.1021/acs.biochem.8b00835en
dc.identifier.issn0006-2960
dc.identifier.otherPURE: 256266083
dc.identifier.otherPURE UUID: e6732e98-5e24-4631-b67a-7af566dd0a86
dc.identifier.otherScopus: 85054313454
dc.identifier.otherORCID: /0000-0003-0526-223X/work/49580174
dc.identifier.otherWOS: 000447815900011
dc.identifier.urihttp://hdl.handle.net/10023/18467
dc.description.abstractThe five-membered nitrogen plus heteroatom rings known as azolines or in their oxidized form as azoles are very common in natural products and drugs. The oxidation of thiazoline to thiazole in the cyanobactin class of natural products is one of the several important transformations that are known to alter the biological properties of the compound. The ordering of the various chemical reactions that occur during cyanobactin biosynthesis is not fully understood. The structure of the flavin-dependent enzyme responsible for the oxidation of multiple thiazolines reveals it contains an additional domain that in other enzymes recognizes linear peptides. We characterize the activity of the enzyme on two substrates: one with a peptide leader and one without. Kinetics and biophysics reveal that the leader on the substrate is not recognized by the enzyme. The enzyme is faster on either substrate than the macrocyclase or protease in vitro. The enzyme has a preferred order of oxidation of multiple thiazolines in the same linear peptide.
dc.format.extent7
dc.language.isoeng
dc.relation.ispartofBiochemistryen
dc.rightsCopyright © 2018 American Chemical Society. This work has been made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at: https://doi.org/10.1021/acs.biochem.8b00835en
dc.subjectQD Chemistryen
dc.subjectBiochemistryen
dc.subjectNDASen
dc.subject.lccQDen
dc.titleOxidation of the cyanobactin precursor peptide is independent of the leader peptide and operates in a defined orderen
dc.typeJournal articleen
dc.description.versionPostprinten
dc.contributor.institutionUniversity of St Andrews.School of Chemistryen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.identifier.doihttps://doi.org/10.1021/acs.biochem.8b00835
dc.description.statusPeer revieweden
dc.date.embargoedUntil2019-09-12


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