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

Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 β-lactamases.

Antimicrobial agents and chemotherapy - 1 Nov 2012

Delbrück Heinrich, Bogaerts Pierre, Kupper Michaël B, Rezende de Castro Roberta, Bennink Sandra, Glupczynski Youri, Galleni Moreno, Hoffmann Kurt M, Bebrone Carine

Abstract excerpt

GES-1 is a class A extended-spectrum β-lactamase conferring resistance to penicillins, narrow- and expanded-spectrum cephalosporins, and ceftazidime. However, GES-1 poorly hydrolyzes aztreonam and cephamycins and exhibits very low k(cat) values for carbapenems. Twenty-two GES variants have been discovered thus far, differing from each other by 1 to 3 amino acid substitutions that affect substrate specificity....

Read the complete abstract on PubMed

Topics

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

Share to Acinetobacter baumannii
Share to beta-Lactamase Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to beta-Lactamases

Share to beta-Lactams

Share to Carbapenems

Share to Cephalosporins

Share to Crystallography, X-Ray

Share to Isoenzymes

Source

Open in PubMed Open full text

Identifiers

PMID: 22908160
DOI: 10.1128/AAC.01272-12
PMCID: PMC3486532

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

Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 β-lactamases.PMID 22908160Read ↗

GES-18, a New Carbapenem-Hydrolyzing GES-Type β-Lactamase from Pseudomonas aeruginosa That Contains Ile80 and Ser170 ResiduesSemantic proximity Read ↗

In Vitro Prediction of the Evolution of GES-1 β-Lactamase Hydrolytic ActivitySemantic proximity Read ↗

Kinetic characterization of GES-22 β-lactamase harboring the M169L clinical mutation.Semantic proximity Read ↗

SHV-type beta-lactamases.Semantic proximity Read ↗

GES-13, a beta-lactamase variant possessing Lys-104 and Asn-170 in Pseudomonas aeruginosa.Semantic proximity Read ↗

Unveiling the evolution routes of TEM-type extended-spectrum β-lactamases.Semantic proximity Read ↗

Acquisition of Extended-Spectrum β-Lactamase GES-6 Leading to Resistance to Ceftolozane-Tazobactam Combination in Pseudomonas aeruginosaSemantic proximity Read ↗

Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure.Semantic proximity Read ↗

Extended-spectrum beta-lactamases: structure and kinetic mechanism.Semantic proximity Read ↗

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

Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability.Semantic proximity Read ↗

Roles of residues Cys69, Asn104, Phe160, Gly232, Ser237, and Asp240 in extended-spectrum beta-lactamase Toho-1.Semantic proximity Read ↗

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