Characterization of the new AmpC beta-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 loop that affects ceftazidime hydrolysis.
Perez-Llarena, Francisco Jose; Kerff, Frédéric; Zamorano, Lauraet al.
2013 • In Antimicrobial Agents and Chemotherapy, 57 (10), p. 5158-61
[en] A novel class C beta-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 beta-lactamases, the Phe313 residue located in the R2 loop affects ceftazidime hydrolysis and alters the phenotype of E. coli strains carrying this variant.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Perez-Llarena, Francisco Jose
Kerff, Frédéric ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Zamorano, Laura
Fernandez, Maria Carmen
Nunez, Maria Luz
Miro, Elisenda
Oliver, Antonio
Navarro, Ferran
Bou, German
Language :
English
Title :
Characterization of the new AmpC beta-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 loop that affects ceftazidime hydrolysis.
Publication date :
2013
Journal title :
Antimicrobial Agents and Chemotherapy
ISSN :
0066-4804
eISSN :
1098-6596
Publisher :
American Society for Microbiology, Washington, United States - District of Columbia
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