Expanding molecular diversity of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products by radical S-adenosylmethionine (SAM) enzymes: recent advances and mechanistic insights.
10.1016/S1875-5364(25)60845-4
- Author:
Jiawei FENG
1
;
Jiarong MO
1
;
Xinya HEMU
2
Author Information
1. State Key Laboratory of Natural Medicines, School of Traditional Chinese Pharmacy, China Pharmaceutical University, Nanjing 210098, China.
2. State Key Laboratory of Natural Medicines, School of Traditional Chinese Pharmacy, China Pharmaceutical University, Nanjing 210098, China. Electronic address: hemuxinya@cpu.edu.cn.
- Publication Type:Review
- Keywords:
Epimerization;
Methylation;
Radical S-adenosylmethionine;
Ribosomally synthesized and post-translationally modified peptides;
Side-chain cross-linking
- MeSH:
Protein Processing, Post-Translational;
S-Adenosylmethionine/chemistry*;
Ribosomes/metabolism*;
Peptides/metabolism*;
Biological Products/metabolism*;
Humans
- From:
Chinese Journal of Natural Medicines (English Ed.)
2025;23(3):257-268
- CountryChina
- Language:English
-
Abstract:
Ribosomally synthesized and post-translationally modified peptides (RiPPs) constitute a vast and diverse family of bioactive peptides. These peptides, synthesized by ribosomes and subsequently modified by various tailoring enzymes, possess a wide chemical space. Among these modifications, radical S-adenosylmethionine (rSAM) enzymes employ unique radical chemistry to introduce a variety of novel peptide structures, which are crucial for their activity. This review examines the major types of modifications in RiPPs catalyzed by rSAM enzymes, incorporating recent advancements in protein structure analysis techniques and computational methods. Additionally, it elucidates the diverse catalytic mechanisms and substrate selectivity of these enzymes through an analysis of the latest crystal structures.
