GSH-Reductase
Glutathione (GSH)

Author: Gianpiero Pescarmona
Date: 15/10/2009

Description

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";

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