A kinetic analysis of the inhibition of FOX-4 β-lactamase, a plasmid-mediated AmpC cephalosporinase, by monocyclic β-lactams and carbapenems.

@article{PappWallace2014AKA,
  title={A kinetic analysis of the inhibition of FOX-4 $\beta$-lactamase, a plasmid-mediated AmpC cephalosporinase, by monocyclic $\beta$-lactams and carbapenems.},
  author={K. Papp-Wallace and S. Mallo and C. Bethel and M. Taracila and A. Hujer and A. Fern{\'a}ndez and J. Gatta and Kerri M. Smith and Yao-Chang Xu and M. Page and E. Desarbre and G. Bou and R. Bonomo},
  journal={The Journal of antimicrobial chemotherapy},
  year={2014},
  volume={69 3},
  pages={
          682-90
        }
}
OBJECTIVES Class C β-lactamases are prevalent among Enterobacteriaceae; however, these enzymes are resistant to inactivation by commercially available β-lactamase inhibitors. In order to find novel scaffolds to inhibit class C β-lactamases, the comparative efficacy of monocyclic β-lactam antibiotics (aztreonam and the siderophore monosulfactam BAL30072), the bridged monobactam β-lactamase inhibitor BAL29880, and carbapenems (imipenem, meropenem, doripenem and ertapenem) were tested in kinetic… Expand
LN-1-255, a penicillanic acid sulfone able to inhibit the class D carbapenemase OXA-48.
Ceftazidime-Avibactam Resistance Mediated by the N346Y Substitution in Various AmpC β-Lactamases
Kinetics of the Interaction between BAL29880 and LK157 and the Class C β-Lactamase CHE-1
New β-Lactamase Inhibitors in the Clinic.
Genetics of Acquired Antibiotic Resistance Genes in Proteus spp.
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