New mutations in ADC-type β-lactamases from Acinetobacter spp. affect cefoxitin and ceftazidime hydrolysis | Zendy

Astrid Pérez | Zendy; Francisco José Pérez-Llarena | Zendy; Patrícia Guedes Garcia | Zendy; Frédéric Kerff | Zendy; Alejandro Beceiro | Zendy; Moreno Galleni | Zendy; Germán Bou | Zendy

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New mutations in ADC-type β-lactamases from Acinetobacter spp. affect cefoxitin and ceftazidime hydrolysis

Author(s) -

Astrid Pérez,

Francisco José Pérez-Llarena,

Patrícia Guedes Garcia,

Frédéric Kerff,

Alejandro Beceiro,

Moreno Galleni,

Germán Bou

Publication year - 2014

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/dku163

Subject(s) - cefoxitin , ceftazidime , acinetobacter , microbiology and biotechnology , antibiotics , biology , chemistry , bacteria , genetics , pseudomonas aeruginosa , staphylococcus aureus

Two natural variants of ADC-type β-lactamases of Acinetobacter spp., ADC-1 and ADC-5, differ by nine mutations in their protein sequence. ADC-5 hydrolyses cefoxitin better than ADC-1 and the opposite is true for ceftazidime. We produced single and combined mutations in ADC-5 and characterized the variants microbiologically and biochemically to determine which amino acid residues are involved in the hydrolysis of β-lactam antibiotics in this family of β-lactamases.

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