Glutathione Reductase family (GR)

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Last update: 2021-12-02 (Bruno Savelli)

Glutathione Reductase family (GR)


Glutathione reductase (GR) (EC, also known as glutathione-disulfide reductase (GSR), catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH). They function as dimeric disulfide oxidoreductase and utilize an FAD prosthetic group and NADPH. They are defined thank to a small NADH binding domain within a larger FAD binding domain. GR sequences are closely related to dihydrolipoamide dehydrogenase.
The GR are conserved between all kingdoms. In bacteria, yeasts, and animals, only one glutathione reductase gene has been detected. Two GR genes have been found in green organisms. Drosophila and Trypanosomes do not possess GR encoding sequence.


Glutathione Reductase Family : Pfam: PF07992
Pyridine nucleotide-disulphide oxidoreductase (Common with MDAR family) PF02852
Pyr_redox_dim. Interpro: IPR023753
FAD/NAD(P)-binding domain IPR016156
FAD/NAD-linked_Rdtase_dimer. IPR006324
Glut-diS_reduct. IPR004099
Pyr_nucl-diS_OxRdtase_dimer. IPR012999


Rouhier N, Couturier J, Jacquot JP. Genome-wide analysis of plant glutaredoxin systems. J Exp Bot. 2006;57(8):1685-96. PMID: 16720602.
Trivedi DK, Gill SS, Yadav S, Tuteja N. Genome-wide analysis of glutathione reductase (GR) genes from rice and Arabidopsis. Plant Signal Behav. 2013 Feb;8(2):e23021. PMID: 23221779