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.[
1. FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
2. CATALYTIC ACTIVITY: 2 glutathione + NADP = glutathione disulfide + NADPH.
3. COFACTOR: Binds 1 FAD per subunit.
4. SUBUNIT: Homodimer; disulfide-linked.
5. SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm.
6. ALTERNATIVE PRODUCTS: Event=Alternative initiation; Named isoforms=2; Name=Mitochondrial; IsoId=P00390-1; Sequence=Displayed; Name=Cytoplasmic; IsoId=P00390-2; Sequence=VSP_018972; Note=Initiator Met-1 is removed. Contains a N-acetylalanine at position 2;
7. DOMAIN: Each subunit can be divided into 4 domains that are consecutive along the polypeptide chain. Domains 1 and 2 bind FAD and NADPH, respectively. Domain 4 forms the interface.
8. PTM: The initiator Met-1 of isoform Cytoplasmic is removed. Isoform Cytoplasmic is acetylated at position 2.
9. MISCELLANEOUS: The active site is a redox-active disulfide bond.
10. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
11. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/gsr/";
12. WEB RESOURCE: Name=Wikipedia; Note=Glutathione reductase entry; URL="http://en.wikipedia.org/wiki/Glutathione_reductase";
