Epoxypeptide antibiotic tetaine mimics peptides in transport to bacteria
| Autor: | Barbara Woynarowska, Henryk Chmara, Edward Borowski |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Pharmacology
Oligopeptide Lysis Bacteria Permease Biological Transport Dipeptides Tripeptide Biology medicine.disease_cause Anti-Bacterial Agents Microbiology chemistry.chemical_compound Bacteriolysis chemistry Biochemistry Staphylococcus aureus Drug Discovery Escherichia coli medicine Peptidoglycan Diaminopimelic acid Oligopeptides |
| Zdroj: | The Journal of Antibiotics. 34:1608-1612 |
| ISSN: | 1881-1469 0021-8820 |
| DOI: | 10.7164/antibiotics.34.1608 |
| Popis: | Tetaine induced the lysis of Escherichia coli cells. Several di- and tripeptides were found to protect this cells against tetaine action. Certain peptides are able to diminish the inhibition by tetaine of diaminopimelic acid incorporation into peptidoglycan and the extent of this corresponds to the protection of the cells against the tetaine-induced lysis. The data indicate that tetaine enters E. coli cells predominantly by dipeptide permease and in part by one or more oligopeptide permease system. A number of di- and tripeptides diminished the inhibitory effect of tetaine on the incorporation of lysine into peptidoglycan of Staphylococcus aureus Oxford. In contrast to E. coli, tetaine seems to be transported into S. aureus by a single transport system. |
| Databáze: | OpenAIRE |
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