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The cyclic structure of the enterococcal peptide antibiotic AS‐48
Author(s) -
Samyn Bart,
Martinez-Bueno Manuel,
Devreese Bart,
Maqueda Mercedes,
Gálvez Antonio,
Valdivia Eva,
Coyette Jacques,
Van Beeumen Jozef
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00925-2
Subject(s) - peptide , enterococcus faecalis , cyclic peptide , peptide bond , chemistry , mass spectrometry , antibiotics , molecular mass , biochemistry , stereochemistry , chromatography , enzyme , escherichia coli , gene
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.