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

Peroxiredoxin 6 homodimerization and heterodimerization with glutathione S-transferase pi are required for its peroxidase but not phospholipase A2 activity.

Free radical biology & medicine - 1 May 2016

Zhou Suiping, Sorokina Elena M, Harper Sandra, Li Haitao, Ralat Luis, Dodia Chandra, Speicher David W, Feinstein Sheldon I, Fisher Aron B

Abstract excerpt

Peroxiredoxin 6 (Prdx6) is a unique 1-Cys member of the peroxiredoxin family with both GSH peroxidase and phospholipase A2 (PLA2) activities. It is highly expressed in the lung where it plays an important role in antioxidant defense and lung surfactant metabolism. Glutathionylation of Prdx6 mediated by its heterodimerization with GSH S-transferase π (πGST) is required for its peroxidatic catalytic cycle....

Read the complete abstract on PubMed

Topics

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

Share to Antioxidants
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Glutathione S-Transferase pi

Share to Oxidation-Reduction

Share to Peroxidase

Share to Phospholipases A2

Share to Pulmonary Surfactants

Source

Open in PubMed Open full text

Identifiers

PMID: 26891882
DOI: 10.1016/j.freeradbiomed.2016.02.012
PMCID: PMC4844822

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

Peroxiredoxin 6 homodimerization and heterodimerization with glutathione S-transferase pi are required for its peroxidase but not phospholipase A2 activity.PMID 26891882Read ↗

Structure and phospholipase function of peroxiredoxin 6: identification of the catalytic triad and its role in phospholipid substrate binding.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 ↗

Allelic variants of glutathione S-transferase P1-1 differentially mediate the peroxidase function of peroxiredoxin VI and alter membrane lipid peroxidation.Semantic proximity Read ↗

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 ↗

A novel lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6.Semantic proximity Read ↗

Structural basis for catalytic activity and enzyme polymerization of phospholipid hydroperoxide glutathione peroxidase-4 (GPx4).Semantic proximity Read ↗

Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2.Semantic proximity Read ↗

Mitogen-activated protein kinase-mediated phosphorylation of peroxiredoxin 6 regulates its phospholipase A(2) activity.Semantic proximity Read ↗

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

Conserved cysteine residues provide a protein-protein interaction surface in dual oxidase (DUOX) proteins.Semantic proximity Read ↗

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

Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.Semantic proximity Read ↗

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