- Characterization of the new AmpC β-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 loop that affects ceftazidime hydrolysis.
Characterization of the new AmpC β-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 loop that affects ceftazidime hydrolysis.
Antimicrobial agents and chemotherapy (2013-07-24)
Francisco José Pérez-Llarena, Frédéric Kerff, Laura Zamorano, María Carmen Fernández, Maria Luz Nuñez, Elisenda Miró, Antonio Oliver, Ferran Navarro, Germán Bou
PMID23877692
ZUSAMMENFASSUNG
A novel class C β-lactamase (FOX-8) was isolated from a clinical strain of Escherichia coli. The FOX-8 enzyme possessed a unique substitution (Phe313Leu) compared to FOX-3. Isogenic E. coli strains carrying FOX-8 showed an 8-fold reduction in resistance to ceftazidime relative to FOX-3. In a kinetic analysis, FOX-8 displayed a 33-fold reduction in kcat/Km for ceftazidime compared to FOX-3. In the FOX family of β-lactamases, the Phe313 residue located in the R2 loop affects ceftazidime hydrolysis and alters the phenotype of E. coli strains carrying this variant.