Evan T. Miller, Oleg V. Tsodikov and Sylvie Garneau-Tsodikova
Nat. Prod. Rep., 2024,41, 113-147
Abstract
This review unpacks the accumulated knowledge of the structural bases of the unique properties and capabilities of DMATS-type prenyltransferases (PTs) that make them promising biocatalysts.
Fan Zhang, Di Zhao, Yuzhu Wu and Lei Li
Nat. Prod. Rep., 2025,42, 1303-1343
Abstract
This review highlights the occurrence, structures, biosynthesis and bioactivities of prenylated bacterial natural products and outlines the mechanistic study of cluster-situated prenyltransferases for the development of novel biocatalysts.
Florian Hubrich
Nat. Prod. Rep., 2026, Advance Article
Abstract
This review highlights advances in the field of amino acid and peptide prenyltransferases, underscoring their value for chemoenzymatic peptide late-stage functionalization and drug development and showcasing their scope, promiscuity and engineering.
Yi Du, Iman Korchi, Aleksandr E. Rubtsov and Andrei V. Malkov
New J. Chem., 2023,47, 20358-20362
Abstract
Prenylated polyphenols occur naturally and exhibit biological activity superior to the ubiquitous parent polyphenols.
Kiall F. Suazo, Jakub Bělíček, Garrett L. Schey, Shelby A. Auger, Alexandru M. Petre, Ling Li, Katarzyna M. Błażewska, David Kopečný and Mark D. Distefano
RSC Chem. Biol., 2023,4, 913-925
Abstract
Protein prenylation typically involves linkage of the lipid via a thioether bond. Here we report the discovery of prenoylation, a thioester-linked modification. In the case of ALDH9A1, this modification may serve an important regulatory function.