Glutathione reductase, also known as GSR or GR, is an enzyme (EC 1.8.1.7) that reduces glutathione disulfide (GSSG) to the sulfhydryl form GSH, which is an important cellular antioxidant.
For every mole of oxidized glutathione (GSSG), one mole of NADPH is required to reduce GSSG to GSH. The enzyme forms a FAD-bound homodimer. 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.
Read more about Glutathione Reductase: Reaction Mechanism of Human Glutathione Reductase, Glutathione Reductase in Human Cells, Monitoring Glutathione Reductase Activity