Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Eglin c | - |
synthetic construct |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
synthetic construct | - |
- |
- |
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 | ? | - |
? |