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Literature summary for 5.2.1.8 extracted from
- The periplasmic peptidyl prolyl cis-trans isomerases PpiD and SurA have partially overlapping substrate specificities (2008), FEBS J., 275, 3470-3479.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | - |
Escherichia coli | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
isoform PpiD | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | PpiD interacts with misfolded proteins such as scrambled ribonuclease A or with D-somatostatin, with the amino acid sequence AGSKNFFWKTFTSS, and derived model peptides. Substrate specificity of PpiD is less specific than that for isoform SurA. The substrate specificity of PpiD is determined more by the hydrophobicity of residues in the model peptides than the presence of aromatic residues | Escherichia coli | ? | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | PpiD interacts with misfolded proteins such as scrambled ribonuclease A or with D-somatostatin, with the amino acid sequence AGSKNFFWKTFTSS and derived model peptides | Escherichia coli |
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