CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.50 | FAD/NAD(P)-binding domain |
|
3.50.50.60 | FAD/NAD(P)-binding domain |
Domain Context
CATH Clusters
| Superfamily | FAD/NAD(P)-binding domain |
| Functional Family | Glutathione reductase |
Enzyme Information
| 1.8.1.16 |
Glutathione amide reductase.
based on mapping to UniProt D0VWY5
2 glutathione amide + NAD(+) = glutathione amide disulfide + NADH.
-!- The enzyme restores glutathione amide disulfide, which is produced during the reduction of peroxide by EC 1.11.1.17 back to glutathione amide (it catalyzes the reaction in the opposite direction to that shown). -!- The enzyme belongs to the family of flavoprotein disulfide oxidoreductases, but unlike other members of the family, which are specific for NADPH, it prefers NADH.
|
UniProtKB Entries (1)
| D0VWY5 |
GASHR_MARGR
Marichromatium gracile
Glutathione amide reductase
|
PDB Structure
| PDB | 2R9Z |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Understanding nicotinamide dinucleotide cofactor and substrate specificity in class I flavoprotein disulfide oxidoreductases: crystallographic analysis of a glutathione amide reductase.
J.Mol.Biol.
|
