Prenylation of a nonaromatic carbon of indolylbutenone by a fungal indole prenyltransferase.
FtmPT1 from Aspergillus fumigatus is a fungal indole prenyltransferase (PT) that normally catalyzes the regiospecific prenylation of brevianamide F (cyclo-L-Trp-L-Pro) at the C-2 position of the indole ring with dimethylallyl diphosphate (DMAPP). Interestingly, FtmPT1 exhibited remarkable substrate tolerance and accepted (E)-4-(1H-indol-3-yl)but-3-en-2-one (1) as a substrate to produce an unnatural novel α-prenylindolylbutenone (1a). This is the first demonstration of the prenylation of a nonaromatic carbon of the acceptor substrate by a fungal indole PT.
Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Tokyo 113-0033, Japan.
Jing
J
Chen
Hiroyuki
H
Morita
Toshiyuki
T
Wakimoto
Takahiro
T
Mori
Hiroshi
H
Noguchi
Ikuro
I
Abe
D000475:Alkenes / Q000737:chemistry* / Q000378:metabolism; D001232:Aspergillus fumigatus / Q000201:enzymology*; D055162:Biocatalysis; D002244:Carbon / Q000737:chemistry* / Q000378:metabolism; D004122:Dimethylallyltranstransferase / Q000378:metabolism*; D007211:Indoles / Q000737:chemistry / Q000378:metabolism; D054876:Prenylation; D013379:Substrate Specificity
D000475:Alkenes; D007211:Indoles; C558934:butylene; D002244:Carbon; C030374:indole; D004122:Dimethylallyltranstransferase