ArticleAntimicrobial agents and chemotherapy2012
Kinetic and crystallographic studies of extended-spectrum GES-11, GES-12, and GES-14 β-lactamases.
Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Quantitative interpretation models for targeted next-generation sequencing in lower respiratory tract infections: a multicenter prospective study.Respiratory research · 2026Article
- Structural comparison of substrate-binding pockets of serine β-lactamases in classes A, C, and D.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Imipenem/Relebactam Resistance in Clinical Isolates of Extensively Drug Resistant Pseudomonas aeruginosa: Inhibitor-Resistant β-Lactamases and Their Increasing Importance.Antimicrobial agents and chemotherapy · 2022Article
- High prevalence ofAIMS microbiology · 2022Article
- Molecular Epidemiology of Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2020Article
- Freshwater viral metagenome reveals novel and functional phage-borne antibiotic resistance genes.Microbiome · 2020Article
- Targeting the Class A Carbapenemase GES-5 via Virtual Screening.Biomolecules · 2020Article
- Extensively Drug-ResistantOpen forum infectious diseases · 2019Article
- Deciphering Multifactorial Resistance Phenotypes inMolecular & cellular proteomics : MCP · 2018Article
- GES-14-Producing Acinetobacter baumannii Isolates in a Neonatal Intensive Care Unit in Tunisia Are Associated with a Typical Middle East Clone and a Transferable Plasmid.Antimicrobial agents and chemotherapy · 2017Article
- Kinetic characterization of GES-22 β-lactamase harboring the M169L clinical mutation.The Journal of antibiotics · 2016Article
- A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes.Clinical microbiology reviews · 2016Review
- In vitro prediction of the evolution of GES-1 β-lactamase hydrolytic activity.Antimicrobial agents and chemotherapy · 2015Article
- Kinetic and structural requirements for carbapenemase activity in GES-type β-lactamases.Biochemistry · 2015Article
- Evaluation of clonality and carbapenem resistance mechanisms among Acinetobacter baumannii-Acinetobacter calcoaceticus complex and Enterobacteriaceae isolates collected in European and Mediterranean countries and detection of two novel β-lactamases, GES-22 and VIM-35.Antimicrobial agents and chemotherapy · 2014Article
- GES-18, a new carbapenem-hydrolyzing GES-Type β-lactamase from Pseudomonas aeruginosa that contains Ile80 and Ser170 residues.Antimicrobial agents and chemotherapy · 2013Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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. GES-11 possesses a Gly243Ala substitution which seems to confer to this variant an increased activity against aztreonam and ceftazidime. GES-12 differs from GES-11 by a single Thr237Ala substitution, while GES-14 differs from GES-11 by the Gly170Ser mutation, which is known to confer increased carbapenemase activity. GES-11 and GES-12 were kinetically characterized and compared to GES-1 and GES-14. Purified GES-11 and GES-12 showed strong activities against most tested β-lactams, with the exception of temocillin, cefoxitin, and carbapenems. Both variants showed a significantly increased rate of hydrolysis of cefotaxime, ceftazidime, and aztreonam. On the other hand, GES-11 and GES-12 (and GES-14) variants all containing Ala243 exhibited increased susceptibility to classical inhibitors. The crystallographic structures of the GES-11 and GES-14 β-lactamases were solved. The overall structures of GES-11 and GES-14 are similar to that of GES-1. The Gly243Ala substitution caused only subtle local rearrangements, notably in the typical carbapenemase disulfide bond. The active sites of GES-14 and GES-11 are very similar, with the Gly170Ser substitution leading only to the formation of additional hydrogen bonds of the Ser residue with hydrolytic water and the Glu166 residue.
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