Kinetic study of the effect of histidines 240 and 164 on TEM-149 enzyme probed by β-lactam inhibitors
| Autor: | Mariagrazia Perilli, Alessia Sabatini, Giuseppe Celenza, Alisia Mancini, Fabrizia Brisdelli, Pierangelo Bellio, Letizia Di Pietro, Bernardetta Segatore, Gianfranco Amicosante, Carlo Bottoni |
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| Rok vydání: | 2014 |
| Předmět: |
Stereochemistry
Kinetics Penicillins beta-Lactams Pharmacology (medical) Pharmacology Infectious Diseases Medicine (all) beta-Lactamases Acylation chemistry.chemical_compound Mechanisms of Resistance medicine Histidine Monobactams chemistry.chemical_classification Carbacephem Dissociation constant Enzyme chemistry Carbapenems Lactam Cephamycin medicine.drug |
| Zdroj: | Antimicrobial agents and chemotherapy. 58(10) |
| ISSN: | 1098-6596 |
| Popis: | In the present study, we performed a detailed kinetic analysis of the enzymes TEM-149, TEM-149 H240 , and TEM-149 H164-H240 versus a large panel of inhibitors/inactivators, including penicillins, penems, carbapenems, monobactams, cephamycin, and carbacephem. These compounds behaved as poor substrates versus TEM-149, TEM-149 H240 , and TEM-149 H164-H240 β-lactamases, and the K i (inhibition constant), K (dissociation constant of the Henri-Michaelis complex), k +2 and k +3 (first-order acylation and deacylation constants, respectively), and k +2 / K values were calculated. |
| Databáze: | OpenAIRE |
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