P108: Catalytic promiscuous indole prenyltransferase from Streptomyces coelicolor A3(2)

Prenylated indole alkaloids represent a large family of natural products isolated from various terrestrial and marine organisms such as plants, fungi and bacteria. Recent studies about fungal indole prenyltransferases revealed that these enzymes showed relaxed substrate specificity with respect to various indole derivatives. Because prenylated indole derivatives often possess biological activities clearly distinct from their non-prenylated precursors, the derivatization of indoles by catalytic promiscuous indole prenyltransferases can be a useful strategy to produce a biologically active compounds. Recently, IptA indole prenyltransferase from Streptomyces sp. SN-593 was characterized (J. Bacteriol. 192: 2839, 2010). Because the IptA enzyme accepts various indole derivatives to transfer a dimethylallyl group to C-6 or C-7 of the indole derivatives, the indole prenyltransferase can be used as a tool for chemoenzymatic synthesis of prenylated indole alkaloids. In the present study, we report biochemical characterization of the recombinant indole prenyltransferase SCO7467 from S. coelicolor A3(2) and discuss the unique substrate specificity and regio-selectivity.