4.7 Article

Hydrolysis and Inhibition Profiles of beta-Lactamases from Molecular Classes A to D with Doripenem, Imipenem, and Meropenem

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ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
卷 54, 期 1, 页码 565-569

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AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.01004-09

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The stability of doripenem to hydrolysis by beta-lactamases from molecular classes A to D was compared to the stability for imipenem and meropenem. Doripenem was stable to hydrolysis by extended-spectrum beta-lactamases 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 fourfold faster than imipenem.

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