Pranylation of tyrosine and derivatives by a tryptophan C7-prenyltransferase


7-DMATS from Aspergillus fumigatus and SirD from Leptosphaeria maculans catalyse a C7-prenylation of l-tryptophan and an O-prenylation of l-tyrosine in nature, respectively. SirD was reported to catalyse the C7-prenylation of l-tryptophan and some derivatives thereof in vitro. We report here the O-prenylation of tyrosine and O- or N-prenylation of its derivatives by 7-DMATS. These results provide experimental evidence for the close relationship of tyrosine O- and tryptophan C7-prenyltransferases regarding their substrate and catalytic promiscuity.


Aili Fan, Shu-Ming Li


Tetrahedron Letters

Year, Volume, Page

2014, 55, 5199



Tag Element Regiochemistry Product Substrate Cofactor Enzyme
PTDBREC00245 C Regular 7-DMATS
PTDBREC00246 O Regular SirD
PTDBREC00247 O Regular 7-DMATS
PTDBREC00248 O Regular 7-DMATS
PTDBREC00249 O Regular 7-DMATS
PTDBREC00250 O Regular SirD
PTDBREC00251 N Regular 7-DMATS
PTDBREC00252 O Regular 7-DMATS
PTDBREC00253 O Regular 7-DMATS
PTDBREC00254 O Regular 7-DMATS
PTDBREC00255 C Regular SirD
PTDBREC00256 N Regular SirD
PTDBREC00257 O Regular SirD