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Carbapenemases: the Versatile ß-Lactamases

Johnson & Johnson Pharmaceutical Research & Development, L.L.C., Raritan, New Jersey 08869

Carbapenemases are ß-lactamases with versatile hydrolytic capacities. They have the ability to hydrolyze penicillins, cephalosporins, monobactams, and carbapenems. Bacteria producing these ß-lactamases may cause serious infections in which the carbapenemase activity renders many ß-lactams ineffective. Carbapenemases are members of the molecular class A, B, and D ß-lactamases. Class A and D enzymes have a serine-based hydrolytic mechanism, while class B enzymes are metallo-ß-lactamases that contain zinc in the active site. The class A carbapenemase group includes members of the SME, IMI, NMC, GES, and KPC families. Of these, the KPC carbapenemases are the most prevalent, found mostly on plasmids in Klebsiella pneumoniae. The class D carbapenemases consist of OXA-type ß-lactamases frequently detected in Acinetobacter baumannii. The metallo-ß-lactamases belong to the IMP, VIM, SPM, GIM, and SIM families and have been detected primarily in Pseudomonas aeruginosa; however, there are increasing numbers of reports worldwide of this group of ß-lactamases in the Enterobacteriaceae. This review updates the characteristics, epidemiology, and detection of the carbapenemases found in pathogenic bacteria.

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