Lanthipeptide synthase
Definition:
EC Tree > 3 Hydrolases > 3.13 Acting on carbon-sulfur bonds > 3.13.2 Thioether and trialkylsulfonium hydrolases > 3.13.2.4 lanthipeptide synthase
Lanthipeptide synthase is a post-translationally modifying enzyme of ribosomally synthesised and post-translationally modified peptides (RiPPs) that generates lanthionine and 3-methyllanthionine thioether cross-links in lanthipeptides: it first dehydrates Ser/Thr residues to dehydroalanine/dehydrobutyrine, and then intramolecularly adds the thiol of a Cys residue to the dehydro amino acid, yielding (methyl)lanthionine-bridged peptides. The combined reactions convert a protein-L-serine or protein-L-threonine plus a protein-L-cysteine into the corresponding lanthionine or 3-methyllanthionine cross-link plus water, or convert the dehydro amino acid directly with Cys. By installing the characteristic thioether rings it confers stability and antimicrobial activity on lanthipeptide bacteriocins such as nisin. It appears in viruses and cellular organisms and adopts a lanthionine-forming cyclodehydratase/dehydratase fold.
Lanthipeptide synthase is a post-translationally modifying enzyme of ribosomally synthesised and post-translationally modified peptides (RiPPs) that generates lanthionine and 3-methyllanthionine thioether cross-links in lanthipeptides: it first dehydrates Ser/Thr residues to dehydroalanine/dehydrobutyrine, and then intramolecularly adds the thiol of a Cys residue to the dehydro amino acid, yielding (methyl)lanthionine-bridged peptides. The combined reactions convert a protein-L-serine or protein-L-threonine plus a protein-L-cysteine into the corresponding lanthionine or 3-methyllanthionine cross-link plus water, or convert the dehydro amino acid directly with Cys. By installing the characteristic thioether rings it confers stability and antimicrobial activity on lanthipeptide bacteriocins such as nisin. It appears in viruses and cellular organisms and adopts a lanthionine-forming cyclodehydratase/dehydratase fold.
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