Effect of D240G substitution in a novel ESBL CTX-M-27
| Autor: | C. De Champs, R. Baraduc, C. Recule, D. Sirot, Jacques Sirot, Catherine Chanal, Richard Bonnet |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Microbiology (medical)
Models Molecular Cefotaxime Molecular Sequence Data Ceftazidime Microbial Sensitivity Tests medicine.disease_cause beta-Lactams beta-Lactamases Microbiology Escherichia polycyclic compounds medicine Escherichia coli Humans Pharmacology (medical) Cloning Molecular Escherichia coli Infections Pharmacology chemistry.chemical_classification biology Strain (chemistry) Reverse Transcriptase Polymerase Chain Reaction Escherichia coli Proteins biochemical phenomena metabolism and nutrition bacterial infections and mycoses biology.organism_classification Enterobacteriaceae Anti-Bacterial Agents Kinetics Infectious Diseases Enzyme chemistry Amino Acid Substitution Isoelectric Focusing Bacteria medicine.drug |
| Zdroj: | The Journal of antimicrobial chemotherapy. 52(1) |
| ISSN: | 0305-7453 |
| Popis: | Escherichia coil clinical strain Gre-1 collected in 2000 from a French hospital harboured a novel CTX-M-encoding gene, designated bla CTX-M-27- CTX-M-27 differed from CTX-M-14 only by the substitution D240G and was the third CTX-M enzyme harbouring this mutation after CTX-M-15 and CTX-M-16. The Gly-240-harbouring enzyme CTX-M-27 conferred to E. coli higher MICs of ceftazidime (MIC, 8 versus 1 mglL) than did the Asp-240-harbouring CTX-M-14 enzyme. Comparison of CTX-M-14 and CTX-M-27 showed that residue Gly-240 decreased K m for ceftazidime (205 versus 940 μM), but decreased hydrolytic activity against good substrates, such as cefotaxime (k cat , 113 versus 415 s -1 ), probably owing to the alteration of β3 strand positioning during the catalytic process. |
| Databáze: | OpenAIRE |
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