Show simple item record

dc.contributor.authorElshahawi, Sherif I.
Cao, Hongnan
Shaaban, Khaled A.
Ponomareva, Larissa V.
Subramanian, Thangaiah
Farman, Mark L.
Spielmann, H. Peter
Phillips, George N. Jr.
Thorson, Jon S.
Singh, Shanteri
dc.date.accessioned 2017-08-09T17:13:27Z
dc.date.available 2017-08-09T17:13:27Z
dc.date.issued 2017
dc.identifier.citation Elshahawi, Sherif I., Cao, Hongnan, Shaaban, Khaled A., et al.. "Structure and specificity of a permissive bacterial C-prenyltransferase." Nature Chemical Biology, 13, (2017) Springer Nature: 366-368. https://doi.org/10.1038/nchembio.2285.
dc.identifier.urihttps://hdl.handle.net/1911/96641
dc.description.abstract This 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.language.iso eng
dc.publisher Springer Nature
dc.rights This is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Springer Nature.
dc.title Structure and specificity of a permissive bacterial C-prenyltransferase
dc.type Journal article
dc.citation.journalTitle Nature Chemical Biology
dc.citation.volumeNumber 13
dc.identifier.digital Structure-and-Specificity
dc.type.dcmi Text
dc.identifier.doihttps://doi.org/10.1038/nchembio.2285
dc.identifier.pmcid PMC5362326
dc.identifier.pmid 28166207
dc.type.publication post-print
dc.citation.firstpage 366
dc.citation.lastpage 368


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record