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      Carbapenemases: the versatile beta-lactamases.

      Clinical microbiology reviews

      Anti-Bacterial Agents, metabolism, genetics, classification, analysis, beta-Lactamases, enzymology, Pseudomonas aeruginosa, Plasmids, Molecular Epidemiology, Microbial Sensitivity Tests, Klebsiella pneumoniae, epidemiology, Klebsiella Infections, Hydrolysis, Global Health, Enterobacteriaceae Infections, Enterobacteriaceae, Enterobacter cloacae, Disease Outbreaks, Bacterial Proteins, drug effects, Bacteria, pharmacology

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          Abstract

          Carbapenemases are beta-lactamases with versatile hydrolytic capacities. They have the ability to hydrolyze penicillins, cephalosporins, monobactams, and carbapenems. Bacteria producing these beta-lactamases may cause serious infections in which the carbapenemase activity renders many beta-lactams ineffective. Carbapenemases are members of the molecular class A, B, and D beta-lactamases. Class A and D enzymes have a serine-based hydrolytic mechanism, while class B enzymes are metallo-beta-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 beta-lactamases frequently detected in Acinetobacter baumannii. The metallo-beta-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 beta-lactamases in the Enterobacteriaceae. This review updates the characteristics, epidemiology, and detection of the carbapenemases found in pathogenic bacteria.

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          Author and article information

          Journal
          17630334
          10.1128/CMR.00001-07
          1932750

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