Increasing structure diversity of prenylated diketopiperazine derivates by using a 4-dimethylallyltryptophan synthase


To create structural diversity of prenylated diketopiperazine derivatives, acceptance of cyclic dipeptides was tested using FgaPT2, a prenyltransferase from Aspergillus fumigatus, which catalyses the conversion of L: -tryptophan to 4-dimethylallyl-L: -tryptophan. It could be shown that seven tryptophan-containing cyclic dipeptides were accepted by FgaPT2 at high protein concentrations and regiospecifically converted to their C4 prenylated derivatives. The structures of the enzymatic products were elucidated by NMR and LC-MS analyses. This substrate promiscuity of a dimethylallyltryptophan synthase towards cyclic dipeptides increases the potential of the fungal indole prenyltransferases as tools for the production of biologically active compounds.


Nicola Steffan, Shu-Ming Li


Archives of Microbiology

Year, Volume, Page

2009, 191, 461



Tag Element Regiochemistry Product Substrate Cofactor Enzyme
PTDBREC00079 C Regular FgaPT2
PTDBREC00080 C Regular FgaPT2
PTDBREC00081 C Regular FgaPT2
PTDBREC00082 C Regular FgaPT2
PTDBREC00083 C Regular FgaPT2