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

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

Antimicrobial agents and chemotherapy - 1 Jun 2017

Ruggiero Melina, Curto Lucrecia, Brunetti Florencia, Sauvage Eric, Galleni Moreno, Power Pablo, Gutkind Gabriel

Abstract excerpt

PER-2 accounts for up to 10% of oxyimino-cephalosporin resistance in Klebsiella pneumoniae and Escherichia coli in Argentina and hydrolyzes both cefotaxime and ceftazidime with high catalytic efficiencies (kcat/Km ). Through crystallographic analyses, we recently proposed the existence of a hydrogen bond network connecting Ser70-Gln69-oxyanion water-Thr237-Arg220 that might be important for the activity and...

Read the complete abstract on PubMed

Topics

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

Share to beta-Lactamase Inhibitors
Share to beta-Lactamases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cefotaxime

Share to Ceftazidime

Share to Cephalosporins

Share to Clavulanic Acid

Share to Klebsiella pneumoniae

Share to Microbial Sensitivity Tests

Source

Open in PubMed Open full text

Identifiers

PMID: 28320728
DOI: 10.1128/AAC.02193-16
PMCID: PMC5444140

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

Impact of Mutations at Arg220 and Thr237 in PER-2 β-Lactamase on Conformation, Activity, and Susceptibility to Inhibitors.PMID 28320728Read ↗

Insights into structure and activity relationship of clinically mutated PER1 and PER2 class A β-lactamase enzymes.Semantic proximity Read ↗

Comprehensive exploration of the translocation, stability and substrate recognition requirements in VIM-2 lactamaseSemantic proximity Read ↗

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

A drug-resistant β-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency.Semantic proximity Read ↗

Comprehensive exploration of the translocation, stability and substrate recognition requirements in VIM-2 lactamase.Semantic proximity Read ↗

Natural Variants of the KPC-2 Carbapenemase have Evolved Increased Catalytic Efficiency for Ceftazidime Hydrolysis at the Cost of Enzyme Stability.Semantic proximity Read ↗

Mode of Action of the Monobactam LYS228 and Mechanisms Decreasing In Vitro Susceptibility in Escherichia coli and Klebsiella pneumoniae.Semantic proximity Read ↗

A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis.Semantic proximity Read ↗

Insights into β-lactamases from Burkholderia species, two phylogenetically related yet distinct resistance determinants.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 ↗

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

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