The cyclic structure of the enterococcal peptide antibiotic AS-48.
The complete primary structure of the peptide antibiotic AS-48 produced by Enterococcus faecalis has been determined by chemical degradation analysis. The cyclic nature of this 70 residues containing peptide was demonstrated by plasma desorption mass analysis of the generated peptides and electrospray ionisation mass analysis of the native polypeptide. As far as we know, this is the first example of an antibiotic protein cyclised by a tail-head peptide bond formation and not by branching of the polypeptide side chains.
Samyn
B
B
Department of Biochemistry, Physiology and Microbiology, University Gent, Belgium.
Martinez-Bueno
M
M
Devreese
B
B
Maqueda
M
M
Gálvez
A
A
Valdivia
E
E
Coyette
J
J
Van Beeumen
J
J
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D001426:Bacterial Proteins; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics; D010455:Peptides; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000235:genetics; D017421:Sequence Analysis
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D010446:Peptide Fragments; D010455:Peptides; D010456:Peptides, Cyclic; C051034:BacA protein, Enterococcus faecalis