title: Kinetics study of KPC-3, a plasmid-encoded class A carbapenem-hydrolyzing beta-lactamase.
abstract: 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/K)m = 3.48 microM(-1) s(-1)). The efficiency of the enzyme was similar for imipenem and meropenem (k(cat)/K(m), 1.4 and 1.94 microM(-1) s(-1), respectively).
authors.affiliation: Department of Microbiology, Toho University School of Medicine, 5-21-16 Omori-nishi, Ota-ku, Tokyo 1438540, Japan.
authors.forename: Jimena
authors.initials: J
authors.lastname: Alba
authors.forename: Yoshikazu
authors.initials: Y
authors.lastname: Ishii
authors.forename: Kenneth
authors.initials: K
authors.lastname: Thomson
authors.forename: Ellen Smith
authors.initials: ES
authors.lastname: Moland
authors.forename: Keizo
authors.initials: K
authors.lastname: Yamaguchi
mesh_terms: D000595:Amino Acid Sequence; D015780:Carbapenems / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D006868:Hydrolysis; D007700:Kinetics; D001618:beta-Lactamases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D015780:Carbapenems; C434283:beta-lactamase KPC-1; C491478:beta-lactamase KPC-2; D001618:beta-Lactamases