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https://hdl.handle.net/2183/49832 Characterization of the New AmpC β-Lactamase FOX-8 Reveals a Single Mutation, Phe313Leu, Located in the R2 Loop That Affects Ceftazidime Hydrolysis
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Pérez-Llarena, Francisco J.
Kerff, Frédéric
Zamorano, Laura
Fernández-López, María del Carmen
Núñez, María Luz
Miró, Elisenda
Oliver, Antonio
Navarro, Ferrán
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Pérez-Llarena FJ, Kerff F, Zamorano L, Fernández MC, Nuñez ML, Miró E, Oliver A, Navarro F, Bou G. Characterization of the new AmpC β-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 loop that affects ceftazidime hydrolysis. Antimicrob Agents Chemother. 2013 Oct;57(10):5158-61.
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Abstract
[Abstract] 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.
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