Any feedback?
Literature summary for 5.3.4.1 extracted from
- The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli results from a tense conformation of its oxidized form (1993), J. Mol. Biol., 233, 559-566.
General Stability
| General Stability | Organism |
|---|---|
| reduced enzyme is more stable than oxidized enzyme | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | - |
Escherichia coli | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 21100 | - |
gel filtration | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Proteins | native, reduced or with wrong disulfide bonds | Escherichia coli | Proteins | with correct disulfide bonds | ? |  |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
