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Antimicrobial Agents and Chemotherapy, November 2005, p. 4760-4762, Vol. 49, No. 11
0066-4804/05/$08.00+0     doi:10.1128/AAC.49.11.4760-4762.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Kinetics Study of KPC-3, a Plasmid-Encoded Class A Carbapenem-Hydrolyzing ß-Lactamase

Department of Microbiology and Infectious Diseases, Toho University School of Medicine, 5-21-16 Omori-nishi, Ota-ku, Tokyo 1438540, Japan,¹ Center for Research in Anti-Infectives and Biotechnology, Department of Medical Microbiology and Immunology, Creighton University School of Medicine, Omaha, Nebraska 68178²

Received 8 February 2005/ Returned for modification 12 March 2005/ Accepted 3 August 2005

The kinetic activity of KPC-3, a plasmid-encoded class A carbapenemase, was studied. It hydrolyzed penicillins, cephalosporins, carbapenems, and even sulbactam. The best substrate was cephalothin (k_cat/Km = 3.48 µM^–1 s^–1). The efficiency of the enzyme was similar for imipenem and meropenem (k_cat/K_m, 1.4 and 1.94 µM^–1 s^–1, respectively).

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