Glutathione amide reductase
| Glutathione amide reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.8.1.16 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Glutathione amide reductase (EC 1.8.1.16, GAR) is an enzyme with systematic name glutathione amide:NAD+ oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction
The three substrates of this enzyme are glutathione amide disulfide, reduced nicotinamide adenine dinucleotide (NADH), and a proton. Its products are glutathione amide and oxidised NAD+.[3] Glutathione amide reductase is a dimeric flavoprotein (FAD).
References
[edit]- ↑ Vergauwen B, Pauwels F, Jacquemotte F, Meyer TE, Cusanovich MA, Bartsch RG, Van Beeumen JJ (June 2001). "Characterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling". The Journal of Biological Chemistry. 276 (24): 20890–7. doi:10.1074/jbc.M102026200. PMID 11399772.
- ↑ Vergauwen B, Van Petegem F, Remaut H, Pauwels F, Van Beeumen JJ (February 2002). "Crystallization and preliminary X-ray crystallographic analysis of glutathione amide reductase from Chromatium gracile". Acta Crystallographica Section D. 58 (Pt 2): 339–40. doi:10.1107/s0907444901020303. PMID 11807270.
- ↑ Enzyme 1.8.1.16 at KEGG Pathway Database.
External links
[edit]- Glutathione+amide+reductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
