Hydrolysis and inhibition profiles of beta-lactamases from molecular classes A to D with doripenem, imipenem, and meropenem

Antimicrob Agents Chemother. 2010 Jan;54(1):565-9. doi: 10.1128/AAC.01004-09. Epub 2009 Nov 2.


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.

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Bacteria / drug effects
  • Bacteria / enzymology
  • Carbapenems / pharmacology*
  • Doripenem
  • Enzyme Inhibitors / pharmacology*
  • Hydrolysis
  • Imipenem / pharmacology*
  • Kinetics
  • Meropenem
  • Microbial Sensitivity Tests
  • Thienamycins / pharmacology*
  • beta-Lactamase Inhibitors*


  • Anti-Bacterial Agents
  • Carbapenems
  • Enzyme Inhibitors
  • Thienamycins
  • beta-Lactamase Inhibitors
  • Imipenem
  • Doripenem
  • Meropenem