TY - JOUR
T1 - Structure and specificity of a permissive bacterial C-prenyltransferase
AU - Elshahawi, Sherif I.
AU - Cao, Hongnan
AU - Shaaban, Khaled A.
AU - Ponomareva, Larissa V.
AU - Subramanian, Thangaiah
AU - Farman, Mark L.
AU - Spielmann, H. Peter
AU - Phillips, George N.
AU - Thorson, Jon S.
AU - Singh, Shanteri
N1 - Publisher Copyright:
© 2017 Nature America, Inc., part of Springer Nature. All rights reserved.
PY - 2017/4/1
Y1 - 2017/4/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85011660718&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85011660718&partnerID=8YFLogxK
U2 - 10.1038/nchembio.2285
DO - 10.1038/nchembio.2285
M3 - Article
C2 - 28166207
AN - SCOPUS:85011660718
SN - 1552-4450
VL - 13
SP - 366
EP - 368
JO - Nature Chemical Biology
JF - Nature Chemical Biology
IS - 4
ER -