Dehydroalanyllysine: identical COOH-terminal structures in the peptide antibiotics nisin and subtilin.
The recent finding of alpha,beta-unsaturated amino acid residues by Gross and Morrel in the polypeptide antibiotic nisin has stimulated a wider investigation of other antibiotic peptides, particularly those known to contain lanthionine. Subtilin is similar to nisin in that it polymerizes easily and contains lanthionine and beta-methyl lanthionine. Like nisin it was found to contain a carboxyl terminal dehydroalanyllysine sequence and to be split by the enzyme nisinase. An additional alpha,beta-unsaturated amino acid residue was shown to be present in subtilin by reaction with excess methyl mercaptoacetate and subsequent hydrolysis and amino acid analysis. Nisin contains three dehydropeptide residues.
D000409:Alanine; D000596:Amino Acids / Q000032:analysis; D000900:Anti-Bacterial Agents / Q000032:analysis*; D002850:Chromatography, Gel; D003956:Dialysis; D008239:Lysine; D010447:Peptide Hydrolases
D000596:Amino Acids; D000900:Anti-Bacterial Agents; D010447:Peptide Hydrolases; D008239:Lysine; D000409:Alanine