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Literature summary for 5.3.4.1 extracted from
- Oxidative folding and reductive activities of EhPDI, a protein disulfide isomerase from Entamoeba histolytica (2009), Parasitol. Int., 58, 311-313.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of several functional-Trx-domain mutants, that are affected in their in vivo oxidative folding activity to different extents, overview | Entamoeba histolytica |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Entamoeba histolytica | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the active-site cysteine residues of the functional domains, Trx-domains, are essential for catalysis of disulfide bond formation in polypeptides and proteins, such as the bacterial alkaline phosphatase | Entamoeba histolytica | ? | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDI | - |
Entamoeba histolytica |
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Release 2023.1 (January 2023)
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