Any feedback?
Literature summary for 3.4.22.B70 extracted from
- Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease (2006), Biochem. J., 398, 345-352.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| X-ray structure of SENP1CC603S-SUMO-1 complex at 2.8 A resolution | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C603S | inactive in maturation and de-conjugation reactions | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q9P0U3 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | SENP1 appears catalytically competent in their apo forms. Upon SUMO interaction, local conformational rearrangement of Trp465, His529 and Trp534 occurs, while Cys603 separates from the catalytic triad to attack the carbonyl-C of Gly97 of SUMO. After the cleavage event, SUMO is released from the complex and converted into its apo form ready for the next reaction cycle | Homo sapiens | ? | - |
? |  |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | 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
