Glutathione reductase

Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene. Glutathione reductase (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell. Glutathione reductase functions as dimeric disulfide oxidoreductase and utilizes an FAD prosthetic group and NADPH to reduce one molar equivalent of GSSG to two molar equivalents of GSH:

GSR
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGSR, HEL-75, HEL-S-122m, glutathione reductase, glutathione-disulfide reductase, GR, GSRD
External IDsOMIM: 138300 MGI: 95804 HomoloGene: 531 GeneCards: GSR
Orthologs
SpeciesHumanMouse
Entrez

2936

14782

Ensembl

ENSG00000104687

ENSMUSG00000031584

UniProt

P00390

P47791

RefSeq (mRNA)

NM_001195104
NM_000637
NM_001195102
NM_001195103

NM_010344

RefSeq (protein)

NP_000628
NP_001182031
NP_001182032
NP_001182033

NP_034474

Location (UCSC)Chr 8: 30.68 – 30.73 MbChr 8: 34.14 – 34.19 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

The glutathione reductase is conserved between all kingdoms. In bacteria, yeasts, and animals, one glutathione reductase gene is found; however, in plant genomes, two GR genes are encoded. Drosophila and trypanosomes do not have any GR at all. In these organisms, glutathione reduction is performed by either the thioredoxin or the trypanothione system, respectively.

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