THE CYCLIC STRUCTURE OF THE ENTEROCOCCAL PEPTIDE ANTIBIOTIC AS-48

被引：86

作者：

SAMYN, B

MARTINEZBUENO, M

DEVREESE, B

MAQUEDA, M

GALVEZ, A

VALDIVIA, E

COYETTE, J

VANBEEUMEN, J

机构：

[1] STATE UNIV GHENT,DEPT BIOCHEM PHYSIOL & MICROBIOL,B-9000 GHENT,BELGIUM

[2] UNIV LIEGE,CTR INGN PROT,INST CHIM B6,B-4000 LIEGE,BELGIUM

[3] UNIV GRANADA,FAC CIENCIAS,DEPT MICROBIOL,E-18071 GRANADA,SPAIN

来源：

FEBS LETTERS | 1994年 / 352卷 / 01期

关键词：

PRIMARY STRUCTURE; CYCLIC PEPTIDE; ANTIBIOTIC; MASS ANALYSIS;

D O I：

10.1016/0014-5793(94)00925-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

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页码：87 / 90

页数：4

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