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

Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli.

The Journal of biological chemistry - 25 Apr 1997

Vlamis-Gardikas A, Aslund F, Spyrou G, Bergman T, Holmgren A

Abstract excerpt

Glutaredoxin 2 (Grx2) from Escherichia coli catalyzes GSH-disulfide oxidoreductions via two redox-active cysteine residues, but in contrast to glutaredoxin 1 (Grx1) and glutaredoxin 3 (Grx3), is not a hydrogen donor for ribonucleotide reductase. To characterize Grx2, a chromosomal fragment containing the E. coli Grx2 gene (grxB) was cloned and sequenced. grxB (645 base pairs) is located between the rimJ and pyrC...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Proteins

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

Share to Base Sequence

Share to Cloning, Molecular

Share to Escherichia coli

Share to Genes, Bacterial

Share to Molecular Sequence Data

Share to Mutation

Source

Identifiers

PMID: 9111025
DOI: 10.1074/jbc.272.17.11236

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

Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli.PMID 9111025Read ↗

Characterization of Escherichia coli null mutants for glutaredoxin 2.Semantic proximity Read ↗

A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase.Semantic proximity Read ↗

Cloning and Expression of a Novel Human Glutaredoxin (Grx2) with Mitochondrial and Nuclear IsoformsSemantic proximity Read ↗

Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system.Semantic proximity Read ↗

Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant.Semantic proximity Read ↗

The E. coli monothiol glutaredoxin GrxD forms homodimeric and heterodimeric FeS cluster containing complexes.Semantic proximity Read ↗

Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways.Semantic proximity Read ↗

Quantitative assessment of the determinant structural differences between redox-active and inactive glutaredoxins.Semantic proximity Read ↗

Identification of novel targets of cyanobacterial glutaredoxin.Semantic proximity Read ↗

Role of yeast glutaredoxins as glutathione S-transferases.Semantic proximity Read ↗

Kinetic characterization of wild-type and mutant human thioredoxin glutathione reductase defines its reaction and regulatory mechanisms.Semantic proximity Read ↗

A dicotyledon-specific glutaredoxin GRXC1 family with dimer-dependent redox regulation is functionally redundant with GRXC2.Semantic proximity Read ↗

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