A novel post-translational modification of the peptide antibiotic subtilin : isolation and characterization of a natural variant from Bacillus subtilis A.T.C.C. 6633

• Published in: Biochemical journal 1993-04, Vol.291 (1), p.23-27
• Main Authors: CHAN, W. C, BYCROFT, B. W, LEYLAND, M. L, LU-YUN LIAN, ROBERTS, G. C. K
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Anti-Bacterial Agents; Antibiotics (antibacterial agents, antifungal agents); Antibiotics, microbial producers, chemotherapic agents, antiseptics, disinfecting agents; Applied microbiology; Bacillus subtilis; Bacillus subtilis - chemistry; Bacterial Proteins; Bacteriocins; Biological and medical sciences; Chromatography, High Pressure Liquid; Fundamental and applied biological sciences. Psychology; Genetic Variation; Magnetic Resonance Spectroscopy; Microbiology; Molecular Sequence Data; Molecular Structure; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Peptides; Peptides, Cyclic - chemistry; Peptides, Cyclic - isolation & purification; Peptides, Cyclic - metabolism; Protein Processing, Post-Translational; Spectrometry, Mass, Fast Atom Bombardment; Trypsin - metabolism
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj2910023

A variant of the peptide antibiotic subtilin has been isolated from Bacillus subtilis A.T.C.C. 6633, and its structure has been shown to be [N alpha-succinyl-Trp1]subtilin. The chemical structure of a fragment derived by tryptic hydrolysis of the variant is shown to be N alpha-succinyl-Trp-Lys by 1H and 13C n.m.r., fast-atom-bombardment m.s. and total chemical synthesis [N alpha-Succinyl-Trp1]-subtilin is produced later in the growth of the bacterium than is subtilin; reverse-phase h.p.l.c. analysis shows that after 24 h growth the ratio subtilin/[N alpha-succinyl-Trp1]subtilin is approx. 1:2. Although [N alpha-succinyl-Trp1]subtilin retains significant antibacterial activity, it is 10-20 times less active than subtilin.