The ponA Gene of Enterococcus faecalis JH2-2 Codes for a Low-Affinity Class A Penicillin-Binding Protein
| Autor: | Séverine Hallut, Noureddine Rhazi, André Piette, Colette Duez, Fabrice Bouillenne, Ana Amoroso, Jacques Coyette, Séverine Hubert |
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| Rok vydání: | 2004 |
| Předmět: |
Penicillin binding proteins
Molecular Sequence Data medicine.disease_cause Microbiology Enterococcus faecalis Acylation Bacterial Proteins Glycosyltransferase polycyclic compounds Bacteriology medicine Penicillin-Binding Proteins Molecular Biology Escherichia coli Base Sequence biology Lipid II Glycosyltransferases biochemical phenomena metabolism and nutrition biology.organism_classification Enzymes and Proteins Anti-Bacterial Agents Kinetics Biochemistry Genes Bacterial biology.protein Carrier Proteins Bacteria |
| Zdroj: | Journal of Bacteriology. 186:4412-4416 |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | A soluble derivative of the Enterococcus faecalis JH2-2 class A PBP1 ( * PBP1) was overproduced and purified. It exhibited a glycosyltransferase activity on the Escherichia coli 14 C-labeled lipid II precursor. As a dd- peptidase, it could hydrolyze thiolester substrates with efficiencies similar to those of other class A penicillin-binding proteins (PBPs) and bind β-lactams, but with k 2 / K (a parameter accounting for the acylation step efficiency) values characteristic of penicillin-resistant PBPs. |
| Databáze: | OpenAIRE |
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