Article (Scientific journals)
Kinetic properties of four plasmid-mediated AmpC beta-lactamases.
Bauvois, Cedric; Ibuka, Akiko Shimizu; Celso, Almeida et al.
2005In Antimicrobial Agents and Chemotherapy, 49 (10), p. 4240-6
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Keywords :
beta-Lactamases/biosynthesis/classification/genetics/isolation & purification/metabolism
Abstract :
[en] The heterologous production in Escherichia coli, the purification, and the kinetic characterization of four plasmid-encoded class C beta-lactamases (ACT-1, MIR-1, CMY-2, and CMY-1) were performed. Except for their instability, these enzymes are very similar to the known chromosomally encoded AmpC beta-lactamases. Their kinetic parameters did not show major differences from those obtained for the corresponding chromosomal enzymes. However, the K(m) values of CMY-2 for cefuroxime, cefotaxime, and oxacillin were significantly decreased compared to those of the chromosomal AmpC enzymes. Finally, the susceptibility patterns of different E. coli hosts producing a plasmid- or a chromosome-encoded class C enzyme toward beta-lactam antibiotics are mainly due to the overproduction of the beta-lactamase in the periplasmic space of the bacteria rather than to a specific catalytic profile of the plasmid-encoded beta-lactamases.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Bauvois, Cedric
Ibuka, Akiko Shimizu
Celso, Almeida
Alba, Jimena
Ishii, Yoshikazu
Frère, Jean-Marie ;  Université de Liège > Département des sciences de la vie > Centre d'ingénierie des protéines
Galleni, Moreno ;  Université de Liège - ULiège
Language :
English
Title :
Kinetic properties of four plasmid-mediated AmpC beta-lactamases.
Publication date :
2005
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
Volume :
49
Issue :
10
Pages :
4240-6
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 27 November 2015

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