Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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 - 1 Oct 2013

Pérez-Llarena Francisco José, Kerff Frédéric, Zamorano Laura, Fernández María Carmen, Nuñez Maria Luz, Miró Elisenda, Oliver Antonio, Navarro Ferran, Bou Germán

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Proteins
Share to beta-Lactamases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ceftazidime

Share to Escherichia coli

Share to Hydrolysis

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 23877692
DOI: 10.1128/AAC.00818-13
PMCID: PMC3811397

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of the new AmpC β-lactamase FOX-8 reveals a single mutation, Phe313Leu, located in the R2 loop that affects ceftazidime hydrolysis.PMID 23877692Read ↗

Structural perspectives on clinical β-lactamase inhibitors: From mechanism to resistance.Semantic proximity Read ↗

The New β-LactamasesSemantic proximity Read ↗

Novel plasmid-mediated CMY variant (CMY-192) conferring ceftazidime-avibactam resistance in multidrug-resistant Escherichia coliSemantic proximity Read ↗

Extended-spectrum beta-lactamases: the role of inhibitors in therapy.Semantic proximity Read ↗

&#946;-Lactamases: A Survey of Protein DiversitySemantic proximity Read ↗

Extended-Spectrum Cephalosporinases: Structure, Detection and EpidemiologySemantic proximity Read ↗

Detailed investigation of catalytically important residues of class A β-lactamaseSemantic proximity Read ↗

Evolution of extended-spectrum beta-lactamases by mutation.Semantic proximity Read ↗

Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase.Semantic proximity Read ↗

Functional and structural analyses of amino acid sequence variation in PDC β-lactamase reveal different mechanistic pathways toward cefiderocol resistance in Pseudomonas aeruginosaSemantic proximity Read ↗

Structural Basis of Reduced Susceptibility to Ceftazidime-Avibactam and Cefiderocol in Enterobacter cloacae Due to AmpC R2 Loop DeletionSemantic proximity Read ↗

Resistance to ceftazidime is associated with a S220Y substitution in the omega loop of the AmpC beta-lactamase of a Serratia marcescens clinical isolate.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.