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

Probing the role of Met221 in the unusual metallo-β-lactamase GOB-18.

Inorganic chemistry - 19 Nov 2012

Lisa María-Natalia, Morán-Barrio Jorgelina, Guindón María-Fernanda, Vila Alejandro J

Abstract excerpt

Metallo-β-lactamases (MβLs) are the main mechanism of bacterial resistance against last generation β-lactam antibiotics such as carbapenems. Most MβLs display unusual structural features in their active sites, such as binuclear zinc centers without carboxylate bridging ligands and/or a Cys ligand in a catalytic zinc site. Cys221 is an essential residue for catalysis conserved in B1 and B2 lactamases, while most...

Read the complete abstract on PubMed

Topics

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

Share to beta-Lactamases
Share to Kinetics
Share to Methionine

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

Share to Mutation

Share to Organometallic Compounds

Share to Recombinant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 23113650
DOI: 10.1021/ic301801h
PMCID: PMC3593996

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

Probing the role of Met221 in the unusual metallo-β-lactamase GOB-18.PMID 23113650Read ↗

In vivo impact of Met221 substitution in GOB metallo-β-lactamase.Semantic proximity Read ↗

Broad spectrum antibiotic-degrading metallo-β-lactamases are phylogenetically diverse and widespread in the environmentSemantic proximity Read ↗

Metallo-β-lactamases: Novel Weaponry for Antibiotic Resistance in BacteriaSemantic proximity Read ↗

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

Active-site mutants of class B beta-lactamases: substrate binding and mechanistic study.Semantic proximity Read ↗

A Single Salt Bridge in VIM-20 Increases Protein Stability and Antibiotic Resistance under Low-Zinc Conditions.Semantic proximity Read ↗

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

Engineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.Semantic proximity Read ↗

Metallo‐β‐lactamase structure and functionSemantic proximity Read ↗

Structural Insights for Core Scaffold and Substrate Specificity of B1, B2, and B3 Metallo-β-LactamasesSemantic proximity Read ↗

Targeting Metallo-β-Lactamase Enzymes in Antibiotic ResistanceSemantic proximity Read ↗

Structural and functional characterization of an active site-influencing variant (IMP-1-F218Y) in IMP-1 metallo-β-lactamase.Semantic proximity Read ↗

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