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Literature summary extracted from
- Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible for the NADPH-dependent reduction of the mixed disulfide of coenzyme A and glutathione (1977), Biochim. Biophys. Acta, 484, 268-274.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.8.1.7 | Saccharomyces cerevisiae | - |
baker's yeast | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.8.1.7 | - |
Saccharomyces cerevisiae |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.8.1.7 | 140 | - |
purified enzyme | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.8.1.7 | GSSG + NADPH | mixed disulfide between coenzyme A and glutathione | Saccharomyces cerevisiae | glutathione + NADP+ | - |
? |  |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.8.1.7 | NADPH | - |
Saccharomyces cerevisiae | |
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Release 2023.1 (January 2023)
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