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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
Jimena Alba,1
Yoshikazu Ishii,1*
Kenneth Thomson,2
Ellen Smith Moland,2 and
Keizo Yamaguchi1
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 (kcat/Km = 3.48 µM1 s1). The efficiency of the enzyme was similar for imipenem and meropenem (kcat/Km, 1.4 and 1.94 µM1 s1, respectively).
* Corresponding author. Mailing address: Department of Microbiology, Toho University School of Medicine, 5-21-16 Omori-nishi, Ota-ku, Tokyo 1438540, Japan. Phone: 81-3-3762-4151, ext. 2396. Fax: 81-3-5493-5415. E-mail: yoishii{at}med.toho-u.ac.jp.
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.
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Copyright © 2005 by the American Society for Microbiology. All rights reserved.