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Bacteria producing these \u03b2-lactamases may cause serious infections in which the carbapenemase activity renders many \u03b2-lactams ineffective. Carbapenemases are members of the molecular class A, B, and D \u03b2-lactamases. Class A and D enzymes have a serine-based hydrolytic mechanism, while class B enzymes are metallo-\u03b2-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\n                      <jats:italic>Klebsiella pneumoniae<\/jats:italic>\n                      . The class D carbapenemases consist of OXA-type \u03b2-lactamases frequently detected in\n                      <jats:italic>Acinetobacter baumannii<\/jats:italic>\n                      . The metallo-\u03b2-lactamases belong to the IMP, VIM, SPM, GIM, and SIM families and have been detected primarily in\n                      <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                      ; however, there are increasing numbers of reports worldwide of this group of \u03b2-lactamases in the\n                      <jats:italic>Enterobacteriaceae<\/jats:italic>\n                      . This review updates the characteristics, epidemiology, and detection of the carbapenemases found in pathogenic bacteria.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/cmr.00001-07","type":"journal-article","created":{"date-parts":[[2007,7,13]],"date-time":"2007-07-13T13:19:33Z","timestamp":1184332773000},"page":"440-458","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":2160,"title":["Carbapenemases: the Versatile \u03b2-Lactamases"],"prefix":"10.1128","volume":"20","author":[{"given":"Anne Marie","family":"Queenan","sequence":"first","affiliation":[{"name":"Johnson &amp; Johnson Pharmaceutical Research &amp; Development, L.L.C., Raritan, New Jersey 08869"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen","family":"Bush","sequence":"additional","affiliation":[{"name":"Johnson &amp; Johnson Pharmaceutical Research &amp; Development, L.L.C., Raritan, New Jersey 08869"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_1_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.01351-06"},{"key":"e_1_3_1_3_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/41.5.576"},{"key":"e_1_3_1_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.45.2.583-588.2001"},{"key":"e_1_3_1_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.49.11.4760-4762.2005"},{"key":"e_1_3_1_6_2","doi-asserted-by":"publisher","DOI":"10.1098\/rstb.1980.0049"},{"key":"e_1_3_1_7_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2760269"},{"key":"e_1_3_1_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.39.7.1612"},{"key":"e_1_3_1_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.38.1.40-43.2000"},{"key":"e_1_3_1_10_2","doi-asserted-by":"publisher","DOI":"10.3201\/eid1102.030684"},{"key":"e_1_3_1_11_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/dkh321"},{"key":"e_1_3_1_12_2","doi-asserted-by":"publisher","DOI":"10.7164\/antibiotics.45.542"},{"key":"e_1_3_1_13_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.44.6.1556-1561.2000"},{"key":"e_1_3_1_14_2","doi-asserted-by":"publisher","DOI":"10.1086\/421495"},{"key":"e_1_3_1_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.49.2.776-778.2005"},{"key":"e_1_3_1_16_2","doi-asserted-by":"publisher","DOI":"10.1001\/archinte.165.12.1430"},{"key":"e_1_3_1_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.49.7.3018-3020.2005"},{"key":"e_1_3_1_18_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/dki175"},{"key":"e_1_3_1_19_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/dki425"},{"key":"e_1_3_1_20_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1469-0691.2004.01016.x"},{"key":"e_1_3_1_21_2","first-page":"152","volume":"207","year":"1997","unstructured":"Bush, K. 1997. 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