EC Number   |
Inhibitors |
Structure  |
|---|
   3.4.22.33 | more |
scarcely inhibited by chicken chystatin |
 |
| 3.4.22.33 | more |
enzyme is inhibited by cystatin |
|
| 3.4.22.33 | more |
not inhibited by pepstatin |
|
| 3.4.22.33 | more |
no effect on activity by EDTA |
|
| 3.4.22.33 | more |
stability of bromelain in the presence of EDTA and sodium benzoate; stability of bromelain in the presence of EDTA and sodium benzoate |
|
| 3.4.22.33 | Ca2+ |
noncompetitive inhibition at pH 3.5, while both K-and V-type activations of bromelain are observed in the presence of 0.5 mM Ca2+ at pH 4.5 and pH 7.5 |
  |
| 3.4.22.33 | Cu2+ |
12% residual activity at 0.16 mM |
|
| 3.4.22.33 | Cu2+ |
inhibits casein degradation, complete inhibition |
|
| 3.4.22.33 | Cu2+ |
reduces activity |
|
| 3.4.22.33 | Cu2+ |
competitive inhibition at pH 3.5 with 0.6 mM Cu2+, which changes to an uncompetitive inhibition at pH 4.5 and pH 7.5 |
|
