Article
Phenotypic study of resistance of beta-lactamase-inhibitor-resistant TEM enzymes which differ by naturally occurring variations and by site-directed substitution at Asp276.
Antimicrobial agents and chemotherapy - 1 Jun 1998
Caniça M M, Caroff N, Barthélémy M, Labia R, Krishnamoorthy R, Paul G, Dupret J M
Abstract excerpt
At this time an amino acid substitution at position 276 in the TEM-1 enzyme is associated with an additional substitution at position 69 in natural beta-lactamase-inhibitor-resistant (IRT) beta-lactamases. The effect of the Asn276-->Asp substitution on resistance was assessed with the Asn276Asp v...
Topics
- Amoxicillin
- Cephalosporins
- Enzyme Inhibitors
- Escherichia coli
- Models, Molecular
- Mutagenesis, Site-Directed
- Penicillanic Acid
- Penicillins
- Phenotype
- Tazobactam
- beta-Lactamase Inhibitors
- beta-Lactamases