Interaction between beta-Lactam Antibiotics and Exocellular dd-Carboxypeptidase-Transpeptidase of Streptomyces R61
| Autor: | Mélina Leyh-Bouille, H. R. Perkins, Jean-Marie Ghuysen, Jean-Marie Frère |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
medicine.drug_class
Stereochemistry Antibiotics Kinetics Carboxypeptidases Peptidoglycan Plasma protein binding beta-Lactams Biochemistry Benzylpenicillin Streptomyces chemistry.chemical_compound polycyclic compounds medicine chemistry.chemical_classification biology Substrate (chemistry) Penicillin G biology.organism_classification Anti-Bacterial Agents Cephalosporins Enzyme Carbenicillin chemistry Penicillin V Acyltransferases Protein Binding medicine.drug |
| Zdroj: | European Journal of Biochemistry. 50:203-214 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1974.tb03889.x |
| Popis: | On the basis of steady-state kinetics, inhibition of the exocellular dd-carboxypeptidase-trans-peptidase of Streptomyces R61 by β-lactam antibiotics was competitive with regard to the donor substrate. However, the complexes formed between the Streptomyces R61 enzyme and various β-lactam antibiotics were relatively stable, exhibiting half-lives of 40 to 80 min at 37°C and neutral pH. During breakdown of the complexes the protein underwent reactivation, whereas the released antibiotic molecule was chemically altered. With [14C]benzylpenicillin, the released compound was neither benzylpenicillin nor benzylpenicilloic acid. The properties of the Streptomyces R61 enzyme β-lactam antibiotic complexes were compared with those of the complexes formed between the same antibiotics and either the membrane-bound transpeptidase from Streptomyces R61 or the exocellular dd-carboxypeptidase-transpeptidase of Streptomyces R39. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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