A promiscuous prenyltransferase from Aspergillus oryzae catalyses C-prenylations of hydroxynaphthalenes in the presence of different prenyl donors

Prenyltransferases of the dimethylallyltryptophan synthase (DMATS) superfamily are involved in the biosynthesis of secondary metabolites and show broad substrate specificity towards their aromatic substrates with a high regioselectivity for the prenylation reactions. Most members of this superfamily accepted as prenyl donor exclusively dimethylallyl diphosphate (DMAPP). One enzyme, AnaPT from Neosartorya fischeri, was reported recently to use both DMAPP and geranyl diphosphate (GPP) as prenyl donors. In this study, we demonstrate the acceptance of DMAPP, GPP and farnesyl diphosphate (FPP) by a new member of this superfamily, BAE61387 from Aspergillus oryzae DSM1147, for C-prenylations of hydroxynaphthalenes.

Daniel Pockrandt, Christopher Sack, Tatjana Kosiol, Shu-Ming Li

Applied Microbiology and Biotechnology

2014, 98, 4987