Any feedback?
Literature summary for 5.2.1.8 extracted from
- Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A (2002), Proc. Natl. Acad. Sci. USA, 99, 1899-1904.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| interleukin-2 tyrosine kinase | Homo sapiens | catalytic activity of interleukin-2 tyrosine kinase is inhibited by peptidylprolyl isomerase activity of cyclophilin A. Proline-dependent conformational switch within the interleukin-2 tyrosine kinase SH2 domain regulates substrate recognition and mediates regulatory interactions with the active site of cyclophilin A | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| interleukin-2 tyrosine kinase | catalytic activity of interleukin-2 tyrosine kinase is inhibited by peptidylprolyl isomerase activity of cyclophilin A. Proline-dependent conformational switch within the interleukin-2 tyrosine kinase SH2 domain regulates substrate recognition and mediates regulatory interactions with the active site of cyclophilin A | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Cyclophilin A | - |
Homo sapiens |
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
