ArticleACS central science2025
A Unique Class of Cyclases with a Kinase Fold Catalyzes Enethiol-Mediated Macrocyclization of Aminovinyl-Cysteine Motifs in Lanthipeptides.
Article in ACS central science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
2-Aminovinyl-cysteine (AviCys) motifs represent a unique class of macrocyclic structures found in many ribosomally synthesized and post-translationally modified peptides (RiPPs). Despite their essential role in bioactivity, their biosynthetic machinery, particularly the cyclases catalyzing Avi-(Me)-Cys macrocyclization, has not been fully characterized. Herein, we report the discovery and biosynthetic elucidation of class V lanthipeptides rosin A1-A3, which feature a lanthionine (Lan) macrocycle and a C-terminal 2-aminovinyl-3-methyl-cysteine (AviMeCys) macrocycle. Rosins promote the migration of human foreskin fibroblast (HSF) cells, representing the first examples of lanthipeptides with cell migration-promoting activity. Comprehensive
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