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

Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate.

The Journal of biological chemistry - 7 Jul 2000

Seo M S, Kang S W, Kim K, Baines I C, Lee T H, Rhee S G

Abstract excerpt

Peroxidases of the peroxiredoxin (Prx) family contain a Cys residue that is preceded by a conserved sequence in the NH(2)-terminal region. A new type of mammalian Prx, designated PrxV, has now been identified as the result of a data base search with this conserved Cys-containing sequence. The 162-amino acid PrxV shares only approximately 10% sequence identity with previously identified mammalian Prx enzymes and...

Read the complete abstract on PubMed

Topics

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

Share to Disulfides
Share to Glutaredoxins
Share to Hydrogen Peroxide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to JNK Mitogen-Activated Protein Kinases

Share to Mitogen-Activated Protein Kinases

Share to Peroxidases

Share to Peroxiredoxins

Share to Thioredoxins

Source

Identifiers

PMID: 10751410
DOI: 10.1074/jbc.M001943200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate.PMID 10751410Read ↗

Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle.Semantic proximity Read ↗

Catalytic mechanism of Sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxin.Semantic proximity Read ↗

Molecular basis for the resistance of human mitochondrial 2-Cys peroxiredoxin 3 to hyperoxidation.Semantic proximity Read ↗

Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid.Semantic proximity Read ↗

PRDX4, an endoplasmic reticulum-localized peroxiredoxin at the crossroads between enzymatic oxidative protein folding and nonenzymatic protein oxidation.Semantic proximity Read ↗

Peroxiredoxin 1 (Prx1) is a dual-function enzyme by possessing Cys-independent catalase-like activity.Semantic proximity Read ↗

Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4.Semantic proximity Read ↗

Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism.Semantic proximity Read ↗

Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin.Semantic proximity Read ↗

Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological Roles.Semantic proximity Read ↗

Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin.Semantic proximity Read ↗

Unveiling the Significance of Arginine, a second shell conserved residue on structure, stability, and activity of Non- Seleno human Peroxiredoxin 6Semantic proximity Read ↗

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