Structure and Specificity of a Permissive Bacterial C-Prenyltransferase

This study highlights the biochemical and structural characterization of the L-tryptophan C-6 C-prenyltransferase PriB from Streptomyces sp. RM-5-8. PriB was found to be uniquely permissive to a diverse array of prenyl donors and acceptors including the antibiotic daptomycin (Cubicin(®)). This study...

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Detalles Bibliográficos
Autores principales: Elshahawi, Sherif I., Cao, Hongnan, Shaaban, Khaled A., Ponomareva, Larissa V., Subramanian, Thangaiah, Farman, Mark L., Spielmann, H. Peter, Phillips, George N., Thorson, Jon S., Singh, Shanteri
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5362326/
https://www.ncbi.nlm.nih.gov/pubmed/28166207
http://dx.doi.org/10.1038/nchembio.2285
Descripción
Sumario:This study highlights the biochemical and structural characterization of the L-tryptophan C-6 C-prenyltransferase PriB from Streptomyces sp. RM-5-8. PriB was found to be uniquely permissive to a diverse array of prenyl donors and acceptors including the antibiotic daptomycin (Cubicin(®)). This study also highlights two additional PTs (FgaPT2 and CdpNPT) as catalysts for daptomycin prenylation where novel prenylated daptomycins also displayed improved antibacterial activities over the parent drug.

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