The cyclic structure of the enterococcal peptide antibiotic AS-48
| Autor: | Mercedes Maqueda, Bart Devreese, Eva Valdivia, Manuel Martínez-Bueno, Bart Samyn, Jacques Coyette, Antonio Gálvez, Jozef Van Beeumen |
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| Rok vydání: | 1994 |
| Předmět: |
Electrospray
Molecular Sequence Data Primary structure Biophysics Peptide Peptides Cyclic Biochemistry Mass Spectrometry Enterococcus faecalis Mass analysis Bacterial Proteins Structural Biology Genetics Side chain Peptide bond Amino Acid Sequence Molecular Biology Chemical decomposition chemistry.chemical_classification biology Antibiotic Protein primary structure Cell Biology biology.organism_classification Combinatorial chemistry Peptide Fragments Cyclic peptide Anti-Bacterial Agents Molecular Weight chemistry Peptides Sequence Analysis |
| Zdroj: | FEBS Letters. 352:87-90 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(94)00925-2 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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