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Modification by Lanthionine Synthetase AncKC in a Heterologous <i>Escherichia coli</i> System

Nisso Z. MirzoevaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997 Russian FederationSofiya O. PipiyaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997 Russian FederationYuliana A. MokrushinaShemyakin–Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of SciencesMarina V. SerebryakovaA.N. Belozersky Institute of Physicochemical Biology, Moscow, 119991 Russian FederationA. A. GrigorievaCenter of Life Sciences, Skolkovo Institute of Science and TechnologySvetlana DubileyInstitute of Gene Biology, Russian Academy of Sciences, Moscow, 119334 Russian FederationStanislav S. TerekhovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997 Russian FederationI. V. SmirnovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997 Russian Federation
Acta Naturaejournal2024en
Ochiq kirishOlmos

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The increasing resistance of microorganisms to antibiotics makes it a necessity that we search for new antimicrobial agents. Due to their genetically encoded nature, peptides are promising candidates for new antimicrobial drugs. Lantipeptide andalusicin exhibits significant antimicrobial activity against Gram-positive bacteria, making it a promising scaffold for the development of DNA-encoded libraries of lantibiotics. In this study, the modification reaction of andalusicin by class III lanthionine synthetase AncKC was reconstructed in a heterologous Escherichia coli system. The results obtained open possibilities for creating novel peptide-based antimicrobial agents.

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