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 [Accepted]

Abstract

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.

Leibniz-HKI-Authors

Markus Greßler
Dirk Hoffmeister
Tim Schäfer

Identifier

doi: 10.1021/acs.jnatprod.3c01120

PMID: 38231181