Inhibitors | Comment | Organism | Structure |
---|---|---|---|
glutathione | oxidized glutathione leads to enzyme inactivation with simultaneous formation of a mixed disulfide between glutathione and the cysteine residues of enzyme. Enzymical reactivation by glutaredoxin2 in presence of reduced glutathione | Sus scrofa |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Sus scrofa | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Sus scrofa | during oxidative stress, enzyme activity appears to be modulated through enzymatic glutathionylation and deglutathionylation | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sus scrofa | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
oxidized glutathione leads to enzyme inactivation with simultaneous formation of a mixed disulfide between glutathione and the cysteine residues of enzyme. Enzymical reactivation by glutaredoxin2 in presence of reduced glutathione | Sus scrofa |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
heart | - |
Sus scrofa | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | during oxidative stress, enzyme activity appears to be modulated through enzymatic glutathionylation and deglutathionylation | Sus scrofa | ? | - |
? |