Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme
Author:
Funder
Agence Nationale de la Recherche
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
https://www.nature.com/articles/s41589-023-01493-1.pdf
Reference72 articles.
1. Montalban-Lopez, M. et al. New developments in RiPP discovery, enzymology and engineering. Nat. Prod. Rep. 38, 130–239 (2021).
2. Benjdia, A. & Berteau, O. Radical SAM enzymes and ribosomally-synthesized and post-translationally modified peptides: a growing importance in the microbiomes. Front. Chem. 9, 678068 (2021).
3. Benjdia, A. & Berteau, O. Sulfatases and radical SAM enzymes: emerging themes in glycosaminoglycan metabolism and the human microbiota. Biochem. Soc. Trans. 44, 109–115 (2016).
4. Balty, C. et al. Ruminococcin C, an anti-clostridial sactipeptide produced by a prominent member of the human microbiota Ruminococcus gnavus. J. Biol. Chem. 294, 14512–14525 (2019).
5. Balty, C. et al. Biosynthesis of the sactipeptide Ruminococcin C by the human microbiome: mechanistic insights into thioether bond formation by radical SAM enzymes. J. Biol. Chem. 295, 16665–16677 (2020).
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