Structural highlights
Function
A0A182DWE5_9ACTN
Publication Abstract from PubMed
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.
Structure and specificity of a permissive bacterial C-prenyltransferase.,Elshahawi SI, Cao H, Shaaban KA, Ponomareva LV, Subramanian T, Farman ML, Spielmann HP, Phillips GN Jr, Thorson JS, Singh S Nat Chem Biol. 2017 Feb 6. doi: 10.1038/nchembio.2285. PMID:28166207[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Elshahawi SI, Cao H, Shaaban KA, Ponomareva LV, Subramanian T, Farman ML, Spielmann HP, Phillips GN Jr, Thorson JS, Singh S. Structure and specificity of a permissive bacterial C-prenyltransferase. Nat Chem Biol. 2017 Feb 6. doi: 10.1038/nchembio.2285. PMID:28166207 doi:http://dx.doi.org/10.1038/nchembio.2285
