Hydrolysis and Inhibition Profiles of {beta}-Lactamases from Molecular Classes A to D with Doripenem, Imipenem and Meropenem. Antimicrobial agents and chemotherapy [Antimicrob Agents Chemother] Journal article | | Title | Hydrolysis and Inhibition Profiles of {beta}-Lactamases from Molecular Classes A to D with Doripenem, Imipenem and Meropenem. | | Author(s) | Queenan AM, Shang W, Flamm R, Bush K | | Institution | Johnson & Johnson Pharmaceutical Research and Development, L.L.C., 1000 Route 202 South, Raritan NJ 08869. | | Source | Antimicrob Agents Chemother 2009 Nov 2. | | Abstract | Stability of doripenem to hydrolysis by beta-lactamases from molecular classes A-D was compared to imipenem and meropenem. Doripenem was stable to hydrolysis by extended-spectrum beta-lactamases (ESBLs) and AmpC-type beta-lactamases, and demonstrated high affinity for the AmpC enzymes. For the serine carbapenemases, SME-3 and KPC-2, and metallo-beta-lactamases, IMP-1 and VIM-2, doripenem hydrolysis was generally 2 to 150-fold slower than imipenem hydrolysis. SPM-1 hydrolyzed meropenem and doripenem four-fold faster than imipenem. | | Language | ENG | | Pub Type(s) | JOURNAL ARTICLE
| | PubMed ID | 19884379 |
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