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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

 
Queenan AM, Shang W, Flamm R, Bush K 
Hydrolysis and Inhibition Profiles of {beta}-Lactamases from Molecular Classes A to D with Doripenem, Imipenem and Meropenem. [JOURNAL ARTICLE]
Antimicrob Agents Chemother 2009 Nov 2.


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.



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