Pep5: Structure Elucidation of a Large Lantibiotic (pages 616–619)
Dipl.-Chem. Roland Kellner, Prof. Dr. Günther Jung, Michaela Josten, Dipl.-Biochem. Cortina Kaletta, Prof. Dr. Karl-Dieter Entian and Prof. Dr. Hans-Georg Sahl
Article first published online: 30 DEC 2003 | DOI: 10.1002/anie.198906161
Lantibiotics are peptide antibiotics which contain lanthionine. Pep 5, a strongly basic compound, is produced from Staphylococcus epidermidis 5 by ribosomal synthesis of a precursor peptide and post-translational modification. The antibiotic activity of Pep 5 rests on the formation of strain-dependent pores in bacterial membranes. Pep 5 is the hitherto largest lantibiotic (Mr = 3488). It is N-terminally blocked by a 2-oxobutyryl residue and contains, besides 25 protein amino acids, dehydrobutyrine (2), meso-lanthionine (2) and 3-methyllanthionine (1). Automatic Edman degradation, mass spectrometry of enzymatically obtained fragments and chemical derivatization gave a 34-peptide sequence with three sulfide rings (lanthionine = S(CH2CHNH2COOH)2).