Structural similarities of the staphylococcin-like peptide Pep-5 to the peptide antibiotic nisin.
The staphylococcin-like peptide Pep-5 was shown to be a complex mixture of closely related and strongly basic peptides. Five peptides were purified by high-pressure liquid chromatography on reversed-phase and gel filtration columns and further characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and amino acid analysis. Four peptides have molecular weights of ca. 3,500, whereas one is of double size. All contain the thioether amino acid lanthionine and a large number of lysine residues per molecule. The amino terminus of the main active peptide is blocked; the carboxy-terminal end is formed by a lysine residue. The data obtained for Pep-5 suggest striking structural similarities to the peptide antibiotics nisin and subtilin.
D000409:Alanine / Q000031:analogs & derivatives / Q000032:analysis; D000596:Amino Acids / Q000032:analysis; D001430:Bacteriocins / Q000032:analysis*; D002268:Carboxypeptidases; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D009561:Nisin / Q000032:analysis*; D013212:Staphylococcus epidermidis / Q000378:metabolism; D013440:Sulfides
D000596:Amino Acids; D001430:Bacteriocins; D013440:Sulfides; D009561:Nisin; C017724:staphylococcin; D002268:Carboxypeptidases; C001520:lanthionine; D000409:Alanine