BLIP-II Is a Highly Potent Inhibitor of Klebsiella pneumoniae Carbapenemase (KPC-2)
| Autor: | Timothy Palzkill, Dar-Chone Chow, Nicholas G. Brown |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Pharmacology
biology Klebsiella pneumoniae Stereochemistry Chemistry Dissociation rate Microbial Sensitivity Tests biochemical phenomena metabolism and nutrition bacterial infections and mycoses biology.organism_classification beta-Lactamases Microbiology Dissociation constant Bacterial protein Infectious Diseases Bacterial Proteins Carbapenems Mechanisms of Resistance polycyclic compounds Pharmacology (medical) beta-Lactamase Inhibitors Bacteria |
| Zdroj: | Antimicrobial Agents and Chemotherapy. 57:3398-3401 |
| ISSN: | 1098-6596 0066-4804 |
| Popis: | β-Lactamase inhibitory protein II (BLIP-II) is a potent inhibitor of class A β-lactamases. KPC-2 is a class A β-lactamase that is capable of hydrolyzing carbapenems and has become a widespread source of resistance to these drugs for Gram-negative bacteria. Determination of association and dissociation rate constants for binding between BLIP-II and KPC-2 reveals a very tight interaction with a calculated ( k off / k on ) equilibrium dissociation constant of 76 fM (76 × 10 −15 M). |
| Databáze: | OpenAIRE |
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