Description
Product Characteristics:
Glutathione reductase (GR) is a member of pyridine nucleotide- disulfideoxidoreductases, which includes the closely related enzymes thioredoxin reductase, lipoamide dehydrogenase, trypanothione reductase and mercuric ion reductase. GR is a cytoplasmic flavoenzyme widely distributed in aerobic organisms. The dimeric protein is composed of two identical subunits, each containing 1 FAD and 1 redox-active disulfide/dithiol as components of the catalytic apparatus. It plays a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG): GSSG + NADPH + H+?2GSH + NADP+. In mosteukaryotic cells, GR maintains the ratio of [GSH]/[GSSG], and participates in several vital functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis.
Subcellular location: Secreted
Synonyms: glutathione reductase, GLUR, Glutathione reductase mitochondrial, GR, Gr1, GRase, GRD 1, GRD1, GSR, MGC78522.
Target Information: This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. This enzyme is a homodimeric flavoprotein. It is a central enzyme of cellular antioxidant defense, and reduces oxidized glutathione disulfide (GSSG) to the sulfhydryl form GSH, which is an important cellular antioxidant. Rare mutations in this gene result in hereditary glutathione reductase deficiency. Multiple alternatively spliced transcript variants encoding different isoforms have been found. [provided by RefSeq, Aug 2010]