How a Subfamily of Radical S-Adenosylmethionine Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally Modified Peptide Discovery.
Journal
ACS bio & med chem Au
ISSN: 2694-2437
Titre abrégé: ACS Bio Med Chem Au
Pays: United States
ID NLM: 9918232604406676
Informations de publication
Date de publication:
16 Feb 2022
16 Feb 2022
Historique:
medline:
2
12
2021
pubmed:
2
12
2021
entrez:
27
4
2023
Statut:
epublish
Résumé
Radical S-adenosylmethionine (rSAM) enzymes are a large and diverse superfamily of enzymes, some of which are known to participate in the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs). Specifically, a subfamily of rSAM proteins with an elongated C-terminus known as a SPASM domain have become a fixation in the discovery of new RiPP natural products. Arguably, a structural study, a bioinformatic study, and a functional study built the foundation of the research for rSAM-SPASM-protein-modified RiPPs. In this Review, we focus on these three studies and how they initiated what has become an increasingly productive field. In addition, we discuss the current state of RiPPs that depends on rSAM-SPASM proteins and provide guidelines to consider in future research. Lastly, we discuss how genome mining tools have become a powerful means to identify and predict new RiPP natural products. Despite the state of our current knowledge, we do not completely understand the relationship of rSAM-SPASM chemistry, substrate recognition, and the structure-function relationship as it pertains to RiPP biosynthesis, and as such, there remain many interesting findings waiting to be discovered in the future.
Identifiants
pubmed: 37102180
doi: 10.1021/acsbiomedchemau.1c00045
pmc: PMC10114670
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
53-59Informations de copyright
© 2021 The Authors. Published by American Chemical Society.
Déclaration de conflit d'intérêts
The authors declare no competing financial interest.
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