A tripeptide deletion in the R2 loop of the class C -lactamase enzyme FOX-4 impairs cefoxitin hydrolysis and slightly increases susceptibility to -lactamase inhibitors | Zendy

Susana Mallo | Zendy; Francisco José Pérez-Llarena | Zendy; Frédéric Kerff | Zendy; Nelson C. Soares | Zendy; Moreno Galleni | Zendy; Germán Bou | Zendy

Open Access

A tripeptide deletion in the R2 loop of the class C -lactamase enzyme FOX-4 impairs cefoxitin hydrolysis and slightly increases susceptibility to -lactamase inhibitors

Author(s) -

Susana Mallo,

Francisco José Pérez-Llarena,

Frédéric Kerff,

Nelson C. Soares,

Moreno Galleni,

Germán Bou

Publication year - 2010

Publication title -

journal of antimicrobial chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.124

H-Index - 194

eISSN - 1460-2091

pISSN - 0305-7453

DOI - 10.1093/jac/dkq115

Subject(s) - tripeptide , cefoxitin , enzyme kinetics , ceftazidime , enzyme , biology , escherichia coli , imipenem , plasmid , beta lactamase , chemistry , microbiology and biotechnology , biochemistry , stereochemistry , amino acid , active site , antibiotics , bacteria , genetics , antibiotic resistance , gene , pseudomonas aeruginosa , staphylococcus aureus

A natural variant of the AmpC enzyme from Escherichia coli HKY28 with a tripeptide deletion (Gly-286/Ser-287/Asp-288) was recently described. The isolate produced an inhibitor-sensitive AmpC beta-lactamase variant that also conferred higher than usual levels of resistance to ceftazidime in the E. coli host. To demonstrate whether this is true in other class C beta-lactamase enzymes, we deleted the equivalent tripeptide in the FOX-4 plasmid-mediated class C beta-lactamase.

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