Characterization of a new TEM-derived beta-lactamase produced in a Serratia marcescens strain
| Autor: | A De Santis, G. M. Rossolini, Nicola Franceschini, Arduino Oratore, J R Knox, L Pagani, Mariagrazia Perilli, Gianfranco Amicosante, Antonio Felici, F Luzzaro |
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| Rok vydání: | 1997 |
| Předmět: |
Stereochemistry
medicine.medical_treatment Molecular Sequence Data Microbial Sensitivity Tests Penicillins Tripeptide Aztreonam Biology beta-Lactamases chemistry.chemical_compound medicine Pharmacology (medical) Amino Acid Sequence Cloning Molecular Serratia marcescens Antibacterial agent Pharmacology chemistry.chemical_classification Crystallography Base Sequence Strain (chemistry) Drug Resistance Microbial biology.organism_classification Kinetics Infectious Diseases Enzyme chemistry Biochemistry Enzyme inhibitor Mutation Beta-lactamase biology.protein Research Article |
| Zdroj: | Antimicrobial Agents and Chemotherapy. 41:2374-2382 |
| ISSN: | 1098-6596 0066-4804 |
| DOI: | 10.1128/aac.41.11.2374 |
| Popis: | A natural TEM variant beta-lactamase was isolated from an epidemic strain of Serratia marcescens. Nucleotide gene sequencing revealed multiple point mutations located in the 42-to-44 tripeptide and positions 145 to 146, 178, and 238. In addition, a glutamic acid 212 deletion was also found. The purified enzyme was studied from a kinetic point of view, revealing the highest catalytic efficiency (k[cat]/Km) values for ceftazidime and aztreonam compared with the TEM-1 prototype enzyme. The in vitro resistance correlated with kinetic parameters, and the enzyme also mediated resistance to some penicillins and an ampicillin-clavulanic acid combination. The mutational and kinetic changes are discussed in relation to the three-dimensional crystallographic structure of the wild-type TEM-1 enzyme. |
| Databáze: | OpenAIRE |
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