EC Number |
Inhibitors |
Structure |
---|
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 |
|
3.4.22.33 | cystatin |
- |
|
3.4.22.33 | cystatin |
an extended AE-rich N-terminal trunk in secreted pineapple cystatin enhances inhibition of fruit bromelain and is posttranslationally removed during ripening, The AE-rich N-terminal trunk is required to inhibit fruit bromelain (above 95%), whereas its removal decreases inhibition to 20%. Recombinant cystatin containing the complete AE-rich N-terminal trunk and recombinant medium pineapple cystatin effectively inhibit bromelain compared to recombinant core pineapple cystatin |
|
3.4.22.33 | Fe3+ |
reduces activity |
|
3.4.22.33 | Hg2+ |
14% residual activity at 0.16 mM |
|
3.4.22.33 | Hg2+ |
inhibits casein degradation, complete inhibition |
|