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.
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.
Chan
W C
WC
Department of Pharmaceutical Sciences, University of Nottingham, U.K.
Bycroft
B W
BW
Leyland
M L
ML
Lian
L Y
LY
Roberts
G C
GC
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents; D001412:Bacillus subtilis / Q000737:chemistry*; D001426:Bacterial Proteins; D001430:Bacteriocins; D002851:Chromatography, High Pressure Liquid; D014644:Genetic Variation; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D010455:Peptides; D010456:Peptides, Cyclic / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D016339:Spectrometry, Mass, Fast Atom Bombardment; D014357:Trypsin / Q000378:metabolism
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D001430:Bacteriocins; D010446:Peptide Fragments; D010455:Peptides; D010456:Peptides, Cyclic; C080666:subtilin B; D014357:Trypsin; C002836:subtilin