Any feedback?
Literature summary for 3.4.21.66 extracted from
- Predicting proteinase specificities from free energy calculations (2006), J. Mol. Graph. Model., 25, 176-185.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Eglin c | - |
synthetic construct |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| synthetic construct | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | thermitase is characterized by a free cysteine residue near the active site. The enzyme has a preference for large uncharged residues in S1 and S4 (secondary binding pocket). S1S4 binding sites are rather flat, which may explain broad specificity of the enzyme | synthetic construct | ? | - |
? | |
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
