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Lanthipeptide Synthetases Participate the Biosynthesis of 2-Aminovinyl-Cysteine Motifs in Thioamitides
Thioamitides are a group of ribosomally synthesized and post-translational modified peptides with potent antiproliferative and proapoptotic activities. Their biosynthesis remains largely unknown, especially for the characteristic C-terminal 2-aminovinyl-Cysteine (AviCys) motifs. Herein, we report the discovery that homologs of class III lanthipeptide synthetases (LanKCts)encoded outside putative thioamitide biosynthetic gene clusters (BGCs) fully dehydrate the precursor peptides. Remarkably,doi:10.1101/2020.08.21.260323 fatcat:r26hmskvczbt7lrnwfgoz4zo4y