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Literature summary for 5.3.4.1 extracted from
- Reshuffling activity of protein disulfide isomerase reduces refolding yield in the structure-forming step of the oxidative protein folding reaction (2010), Chem. Lett., 39, 263-265.
No PubMed abstract available
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Rattus norvegicus | the oxidoreductase chaperone PDI has an effect on the critical structure-forming step during the oxidative maturation of model disulfide-bond-containing proteins, it inhibits the conformational folding step of oxidative fold maturation and, therefore, has limited overall catalytic efficiency as an oxidoreductase chaperone, impact of rat PDI, null PDI and enzyme domains on the structure-forming step, overview. Detrimental impact of the oxidoreductase activity PDI during conformational folding include peptidyl prolyl isomerase which facilitates cis-trans isomerization of prolines | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the oxidoreductase chaperone PDI has an effect on the critical structure-forming step during the oxidative maturation of model disulfide-bond-containing proteins, it inhibits the conformational folding step of oxidative fold maturation and, therefore, has limited overall catalytic efficiency as an oxidoreductase chaperone, impact of rat PDI, null PDI and enzyme domains on the structure-forming step, overview. Detrimental impact of the oxidoreductase activity PDI during conformational folding include peptidyl prolyl isomerase which facilitates cis-trans isomerization of prolines | Rattus norvegicus | ? | - |
? | |
| additional information | the enzyme renatures denatured RNase A | Rattus norvegicus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PDI | - |
Rattus norvegicus |
| protein disulfide isomerase | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Rattus norvegicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 8.2 | assay at | Rattus norvegicus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | the anomalous behavior of PDI during a key step in oxidative regeneration may contribute to misfolding in the endoplasmic reticulum, aggregation, and neurodegenerative disease | Rattus norvegicus |
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Release 2023.1 (January 2023)
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