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Literature summary for 1.8.1.7 extracted from
- Glutathione reductase from human erythrocytes: amino-acid sequence of the structurally known FAD-binding domain (1981), Eur. J. Biochem., 120, 407-419.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 52500 | - |
2 * 52500 | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| amino acid sequence analysis | Homo sapiens |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+ | substrate and cofactor binding site, three-dimensional structure | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| erythrocyte | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| GSSG + NADPH | - |
Homo sapiens | glutathione + NADP+ | - |
r |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 52500 | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | amino acid sequence of FAD-binding domain | Homo sapiens | |
| FAD | FAD enzyme | Homo sapiens | |
| NADPH | - |
Homo sapiens | |
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Release 2023.1 (January 2023)
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