Heterologous Expression and Characterization of Estercin A, a Class II Lanthipeptide Derived from CF016, with Antimicrobial Activity against Clinically Relevant Pathogens.

Recent genome mining work revealed that unexplored habitats exhibit great potential for discovering new nonribosomal peptides (NRPs) and ribosomally synthesized and post-translationally modified peptides (RiPPs). Lanthipeptides are a group of RiPPs exhibiting a variety of biological functions. They are characterized by the presence of the thioether-containing bis-amino acids lanthionine and/or methyllanthionine.

Biosynthesis of Antimicrobial Ornithine-Containing Lacticin 481 Analogues by Use of a Combinatorial Biosynthetic Pathway in .

Lacticin 481, a ribosomally synthesized and post-translationally modified peptide (RiPP), exhibits antimicrobial activity, for which its characteristic lanthionine and methyllanthionine ring structures are essential. The post-translational introduction of (methyl)lanthionines in lacticin 481 is catalyzed by the enzyme LctM. In addition to macrocycle formation, various other post-translational modifications can enhance and modulate the chemical and functional diversity of antimicrobial peptides.

Synechococsins: Lanthipeptides acting as defensive signals to disarm offensive competitors?

Synechococsins represent a diverse group of class II lanthipeptides from the prochlorosin family, produced by the marine picocyanobacterium Synechococcus. A single strain can produce multiple SyncA peptides through modification by SyncM, a bifunctional lanthipeptide synthetase. Despite the prevalence of these lanthipeptides in nature, their biological functions remain elusive, even for the most studied group, Prochlorococcus MIT9313.

Discovery, Biosynthesis, and Characterization of Rodencin, a Two-Component Lanthipeptide, Harboring d-Amino Acids Introduced by the Unusual Dehydrogenase RodJ.

Lanthipeptides, a group of ribosomally synthesized and post-translationally modified peptides (RiPPs), exhibit diverse structures and bioactivities. Their biosynthetic enzymes serve as valuable tools for peptide bioengineering. Here, we report a class II lanthipeptide biosynthetic gene cluster in a strain, driving the biosynthesis of a two-component lanthipeptide, termed rodencin, featured by the presence of two different d-amino acids, i.