EC Number   |
Metals/Ions |
Reference |
|---|
   3.4.21.1 | Ca2+ |
5 mM, 1.5fold increase in activity, destabilizes the enzyme-pancreatic trypsin inhibitor complex formation |
171878 |
| 3.4.21.1 | Ca2+ |
5 mM, 110% of initial activity |
731841 |
| 3.4.21.1 | Ca2+ |
both chymotrypsin A and B are slightly activated at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 115% and 103% relative activity for chymotrypsin A and B, respectively |
708555 |
| 3.4.21.1 | Ca2+ |
proteolytic activity is 1.5fold enhanced in the presence of 10 mM Ca2+ |
747755 |
| 3.4.21.1 | Ca2+ |
required for catalysis |
707724, 709590 |
| 3.4.21.1 | Cd2+ |
CdCl2 binds to the enzyme mainly via electrostatic forces with binding sites, leading to the increase of alpha-helix and the decrease of beta-sheet. The interaction between CdCl2 and alpha-ChT loosens the protein skeleton and increases the molecular volume of the enzyme. CdCl2 first binds to the interface of the enzyme and then interacts with the key residues His57 or Asp102 or both in the active sites, leading to the activity inhibition of the enzyme under the exposure of high CdCl2 concentrations |
754036 |
| 3.4.21.1 | Co2+ |
5 mM, 120% of initial activity |
731841 |
| 3.4.21.1 | Co2+ |
proteolytic activity is 1.4fold enhanced in the presence of 10 mM Co2+ |
747755 |
| 3.4.21.1 | Mg2+ |
5 mM, 117% of initial activity |
731841 |
| 3.4.21.1 | Mg2+ |
both chymotrypsin A and B are slightly activated at concentrations of 1 and 5 mM. At room temperature, at 5 mM concentration, 111% and 110% relative activity for chymotrypsin A and B, respectively |
708555 |
