Structure and Specificity of a Permissive Bacterial C-prenyltransferase

Authors

Sherif Elshahawi, Chapman UniversityFollow
Hongnan Cao, Rice University
Khaled A. Shaaban, University of Kentucky
Larissa V. Ponomareva, University of Kentucky
Thangaiah Subramanian, University of Kentucky
Mark L. Farman, University of Kentucky
H Peter Spielmann, University of Kentucky
George N. Phillips Jr., Rice University
Jon S. Thorson, University of Kentucky
Shanteri Singh, University of Kentucky

Document Type

Article

Publication Date

2-6-2017

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.

Comments

This article was originally published in Nature Chemical Biology, volume 13, issue 4, in 2017. https://doi.org/10.1038/nchembio.2285

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Recommended Citation

Elshahawi SI, Cao C, Shaaban KA, et al. Structure and specificity of a permissive bacterial C-prenyltransferase. Nat. Chem Biol. 2017;13(4):366-368. https://doi.org/10.1038/nchembio.2285

Copyright

Nature America, Inc.