Parallel evolution of Asco- and Basidiomycete O-Prenyltransferases.

Schäfer T, Haun F, Gressler M, Spiteller P, Hoffmeister D (2024) Parallel evolution of Asco- and Basidiomycete O-Prenyltransferases. J Nat Prod 87(3), 576-582.


Prenyltransferases (PTs) are involved in the biosynthesis of a multitude of pharmaceutically and agriculturally important plant, bacterial, and fungal compounds. Although numerous prenylated compounds have been isolated from Basidiomycota (mushroom-forming fungi), knowledge of the PTs catalyzing the transfer reactions in this group of fungi is scarce. Here, we report the biochemical characterization of an O- and C-prenylating dimethylallyltryptophan synthase (DMATS)-like enzyme LpTyrPT from the scurfy deceiver Laccaria proxima. This PT transfers dimethylallyl moieties to l-tyrosine at the para-O position and to l-tryptophan at atom C-7 and represents the first basidiomycete l-tyrosine PT described so far. Phylogenetic analysis of PTs in fungi revealed that basidiomycete l-tyrosine PTs have evolved independently from their ascomycete counterparts and might represent the evolutionary origin of PTs acting on phenolic compounds in secondary metabolism.


Markus Greßler
Dirk Hoffmeister
Tim Schäfer


doi: 10.1021/acs.jnatprod.3c01120

PMID: 38231181