Structure and specificity of a permissive bacterial C-prenyltransferase

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dc.citation.firstpage366
dc.citation.journalTitleNature Chemical Biology
dc.citation.lastpage368
dc.citation.volumeNumber13
dc.contributor.authorElshahawi, Sherif I.
dc.contributor.authorCao, Hongnan
dc.contributor.authorShaaban, Khaled A.
dc.contributor.authorPonomareva, Larissa V.
dc.contributor.authorSubramanian, Thangaiah
dc.contributor.authorFarman, Mark L.
dc.contributor.authorSpielmann, H.Peter
dc.contributor.authorPhillips, George N.Jr.
dc.contributor.authorThorson, Jon S.
dc.contributor.authorSingh, Shanteri
dc.date.accessioned2017-08-09T17:13:27Z
dc.date.available2017-08-09T17:13:27Z
dc.date.issued2017
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.
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.
dc.identifier.digitalStructure-and-Specificity
dc.identifier.doihttps://doi.org/10.1038/nchembio.2285
dc.identifier.urihttps://hdl.handle.net/1911/96641
dc.language.isoeng
dc.publisherSpringer Nature
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Springer Nature.
dc.titleStructure and specificity of a permissive bacterial C-prenyltransferase
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpost-print
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