Radical SAM-dependent enzymes: Jacks-of-all-trades in RiPP pathways.

Authors

Panagiota-Hanna Koutsandrea, Lorenz Thost, Alicia Courvoisier-Clément, Anna Lisa Vagstad, Silja Mordhorst

Published in

Natural product reports. Sep 15, 2026. Epub Sep 15, 2026.

Abstract

Covering: up to 2026The cofactor S-adenosyl-L-methionine (SAM) plays a key role in the biosynthesis of ribosomally synthesised and post-translationally modified peptide (RiPP) natural products. SAM-dependent enzymes have been shown to catalyse important steps in RiPP biosynthesis, including methylation, desaturation, epimerisation, splicing reactions, and oxidative decarboxylation. Furthermore, a range of SAM-dependent cross-linking reactions result in the formation of complex macrocyclic peptide products, which often exhibit enhanced stability and intriguing biological activities. These post-translational modifications occur in all parts of the peptide molecule, including side chains, peptide backbones, and N- and C-termini. Newly identified RiPP pathways continue to reveal interesting SAM-dependent enzymes that install remarkable chemical moieties. In view of the recent advances in this field, the objective of this review is to provide an overview of the significant chemical diversity of RiPP natural products generated by SAM-dependent enzymes, with a particular focus on post-translational modifications introduced by radical SAM enzymes.

PMID:
42742061
Bibliographic data and abstract were imported from PubMed on 15 Sep 2026.

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