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dc.contributor.authorGkotsi, Danai S.
dc.contributor.authorLudewig, Hannes
dc.contributor.authorSharma, Sunil V.
dc.contributor.authorConnolly, Jack A.
dc.contributor.authorDhaliwal, Jagwinder
dc.contributor.authorWang, Yunpeng
dc.contributor.authorUnsworth, William P.
dc.contributor.authorTaylor, Richard J. K.
dc.contributor.authorMcLachlan, Matthew M. W.
dc.contributor.authorShanahan, Stephen
dc.contributor.authorNaismith, James H.
dc.contributor.authorGoss, Rebecca J. M.
dc.identifier.citationGkotsi , D S , Ludewig , H , Sharma , S V , Connolly , J A , Dhaliwal , J , Wang , Y , Unsworth , W P , Taylor , R J K , McLachlan , M M W , Shanahan , S , Naismith , J H & Goss , R J M 2019 , ' A marine viral halogenase that iodinates diverse substrates ' , Nature Chemistry , vol. 11 , no. 12 , pp. 1091–1097 .
dc.identifier.otherRIS: urn:D947FF951B1BCEA2213FC0C20EDFA21E
dc.identifier.otherRIS: Gkotsi2019
dc.descriptionWe thank the European Research Council under the European Union’s Seventh Framework Programme (FP7/2007–2013/ERC grant agreement no. 614779 GenoChemetics to R.J.M.G.), Syngenta and Wellcome ISSF (grant no. 204821/Z/16/Z to D.S.G.) for generous financial support.en
dc.description.abstractOceanic cyanobacteria are the most abundant oxygen-generating phototrophs on our planet and are therefore important to life. These organisms are infected by viruses called cyanophages, which have recently shown to encode metabolic genes that modulate host photosynthesis, phosphorus cycling and nucleotide metabolism. Herein we report the characterization of a wild-type flavin-dependent viral halogenase (VirX1) from a cyanophage. Notably, halogenases have been previously associated with secondary metabolism, tailoring natural products. Exploration of this viral halogenase reveals it capable of regioselective halogenation of a diverse range of substrates with a preference for forming aryl iodide species; this has potential implications for the metabolism of the infected host. Until recently, a flavin-dependent halogenase that is capable of iodination in vitro had not been reported. VirX1 is interesting from a biocatalytic perspective as it shows strikingly broad substrate flexibility and a clear preference for iodination, as illustrated by kinetic analysis. These factors together render it an attractive tool for synthesis.
dc.relation.ispartofNature Chemistryen
dc.subjectQD Chemistryen
dc.subjectSDG 14 - Life Below Wateren
dc.titleA marine viral halogenase that iodinates diverse substratesen
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.contributor.sponsorEuropean Research Councilen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. University of St Andrewsen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.description.statusPeer revieweden

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