Abstract
The genome sequencing efforts of the first decade of the 21st century have revealed that another major class is formed by ribosomally synthesized and post‐translationally modified peptides (RiPPs). These molecules are produced in all three domains of life, their biosynthetic genes are ubiquitous in the currently sequenced genomes, and their structural diversity is vast. Lantibiotics are examples of this growing class. These peptides are post‐translationally modified to install multiple thioether crosslinks by dehydration of Ser/Thr and subsequent conjugate addition to the dehydro amino acids by Cys thiols. During their biosynthesis, a single enzyme typically breaks 8‐16 chemical bonds and forms 6‐10 new bonds with high control over regio‐ and chemoselectivity. This presentation will focus on how the substrate peptides are recognized by the synthetases and how the enzyme orchestrates the various reactions to generate a single product.
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