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 characterization of GES-22 β-lactamase harboring the M169L clinical mutation.

The Journal of antibiotics - 1 Dec 2016

Saral Aysegul, Leonard David A, Duzgun Azer Ozad, Cicek Aysegul Copur, June Cynthia M, Sandalli Cemal

Abstract excerpt

The class A β-lactamase GES-22 has been identified in Acinetobacter baumannii isolates in Turkey, and subsequently shown to differ from GES-11 by a single substitution (M169L). Because M169 is part of the omega loop, a structure that is known to have major effects on substrate selectivity in class A β-lactamases, we expressed, purified and kinetically characterized this novel variant. Our results show that...

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 Delete account & data About Contact Helena Bioinformatics

Share to Carbapenems

Share to Ceftazidime

Share to Cephalosporins

Share to Clavulanic Acid

Share to Hydrolysis

Share to Penicillins

Source

Open in PubMed Open full text

Identifiers

PMID: 27168312
DOI: 10.1038/ja.2016.48
PMCID: PMC5106332

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Kinetic characterization of GES-22 β-lactamase harboring the M169L clinical mutation.PMID 27168312Read ↗

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

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

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

Structure-function relationships among wild-type variants of Staphylococcus aureus beta-lactamase: importance of amino acids 128 and 216.Semantic proximity Read ↗

Mutation of the conserved Asp-Asp pair impairs the structure, function, and inhibition of CTX-M Class A β-lactamase.Semantic proximity Read ↗

Identification of Arg32Ser, His92Tyr and Leu147Phe novel mutations in chromosomally mediated β-lactamase SHV and in silico characterization to understand their substrate activity imparting resistance.Semantic proximity Read ↗

Inhibition by Avibactam and Clavulanate of the β-Lactamases KPC-2 and CTX-M-15 Harboring the Substitution N132G in the Conserved SDN Motif.Semantic proximity Read ↗

Impact of Mutations at Arg220 and Thr237 in PER-2 β-Lactamase on Conformation, Activity, and Susceptibility to Inhibitors.Semantic proximity Read ↗

SHV-129: A Gateway to Global Suppressors in the SHV β-Lactamase Family?Semantic proximity Read ↗

KPC-12 with a L169M substitution in the Ω loop has reduced carbapenemase activity.Semantic proximity Read ↗

Klebsiella pneumoniae Carbapenemase-2 (KPC-2), Substitutions at Ambler Position Asp179, and Resistance to Ceftazidime-Avibactam: Unique Antibiotic-Resistant Phenotypes Emerge from β-Lactamase Protein Engineering.Semantic proximity Read ↗

Glutamate residues at positions 162 and 164 influence the beta-lactamase activity of SHV-14 obtained from Klebsiella pneumoniae.Semantic proximity Read ↗

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