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Literature summary extracted from
- Chaperone-like activity of peptidyl-prolyl cis-trans isomerase during creatine kinase refolding (2001), Protein Sci., 10, 2346-2353.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.2.1.8 | cyclosporin A | - |
Sus scrofa |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.2.1.8 | Sus scrofa | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.2.1.8 | additional information | isomerase activity of peptidylprolyl isomerase is independent of the chaperone activity. The proper molar ratio is important for the chaperone activity. The cysteine residues of peptidylprolyl isomerase may be a peptide binding site, and may be an essential group for the chaperone function | Sus scrofa | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.2.1.8 | Peptidyl-prolyl cis-trans isomerase | - |
Sus scrofa |
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