Structure and specificity of a permissive bacterial C-prenyltransferase

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dc.citation.firstpage366en_US
dc.citation.journalTitleNature Chemical Biologyen_US
dc.citation.lastpage368en_US
dc.citation.volumeNumber13en_US
dc.contributor.authorElshahawi, Sherif I.en_US
dc.contributor.authorCao, Hongnanen_US
dc.contributor.authorShaaban, Khaled A.en_US
dc.contributor.authorPonomareva, Larissa V.en_US
dc.contributor.authorSubramanian, Thangaiahen_US
dc.contributor.authorFarman, Mark L.en_US
dc.contributor.authorSpielmann, H.Peteren_US
dc.contributor.authorPhillips, George N.Jr.en_US
dc.contributor.authorThorson, Jon S.en_US
dc.contributor.authorSingh, Shanterien_US
dc.date.accessioned2017-08-09T17:13:27Zen_US
dc.date.available2017-08-09T17:13:27Zen_US
dc.date.issued2017en_US
dc.description.abstractThis study highlights the biochemical and structural characterization of the L-tryptophan C6 C-prenyltransferase (C-PT) PriB from Streptomyces sp. RM-5-8. PriB was found to be uniquely permissive to a diverse array of prenyl donors and acceptors including daptomycin. Two additional PTs also produced novel prenylated daptomycins with improved antibacterial activities over the parent drug.en_US
dc.identifier.citationElshahawi, Sherif I., Cao, Hongnan, Shaaban, Khaled A., et al.. "Structure and specificity of a permissive bacterial C-prenyltransferase." <i>Nature Chemical Biology,</i> 13, (2017) Springer Nature: 366-368. https://doi.org/10.1038/nchembio.2285.en_US
dc.identifier.digitalStructure-and-Specificityen_US
dc.identifier.doihttps://doi.org/10.1038/nchembio.2285en_US
dc.identifier.urihttps://hdl.handle.net/1911/96641en_US
dc.language.isoengen_US
dc.publisherSpringer Natureen_US
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Springer Nature.en_US
dc.titleStructure and specificity of a permissive bacterial C-prenyltransferaseen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpost-printen_US
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