The cyclic structure of the enterococcal peptide antibiotic AS‐48

FEBS Letters

Van Beeumen, Jozef³  Martinez-Bueno, Manuel¹  Devreese, Bart³  Samyn, Bart³  Gálvez, Antonio²  Maqueda, Mercedes²  Coyette, Jacques¹  Valdivia, Eva² 

[1] Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie B6, Sart Tilman, B-4000 Liège, Belgium;Departamento de Microbiologia, Facultad de Ciencias, Universidad de Granada, E-18071 Granada, Spain;Department of Biochemistry, Physiology and Microbiology, University Gent, K.L. Ledeganckstraat, 35, B-9000 Gent, Belgium

关键词: Primary structure;    Cyclic peptide;    Antibiotic;    Mass analysis;   

DOI  :  10.1016/0014-5793(94)00925-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown