The complete amino acid sequence of the pediocin-like antimicrobial peptide leucocin C.
The pediocin-like antimicrobial peptide leucocin C produced by a strain of Leuconostoc mesenteroides has been purified using a recently developed rapid two-step procedure. The complete and corrected amino acid sequence of the peptide has been determined by Edman degradation of the intact peptide and a C-terminal fragment generated by cleavage with Asp-N endoprotease. Leucocin C contained 43 residues with the following sequence: KNYGNGVHCTKKGCSVDWGYAWTNIANNSVMNGLTGGNAGWHN. The molecular weight of leucocin C as determined by mass spectrometry was 4595, which is consistent with the theoretical molecular weight of 4596 calculated from the sequence. Moreover, the molecular weights of the two fragments generated by cleavage with Asp-N were also consistent with the determined sequence.
Fimland
Gunnar
G
Department of Biochemistry, University of Oslo, Post Box 1041, Blindern, Oslo, Norway. gunnar.fimland@biokjemi.uio.no
Sletten
Knut
K
Nissen-Meyer
Jon
J
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D001430:Bacteriocins / Q000737:chemistry*; D010450:Endopeptidases / Q000378:metabolism; D019344:Lactic Acid / Q000378:metabolism; D013058:Mass Spectrometry; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D000596:Amino Acids; D001430:Bacteriocins; C464649:leucocin C, Leuconostoc mesenteroides; D019344:Lactic Acid; D010450:Endopeptidases; D008666:Metalloendopeptidases; C058921:endoproteinase Asp-N