EC Number |
Protein Variants |
Reference |
---|
3.4.22.55 | K152A |
mutant enzyme with strikingly altered caspase-2 localization. Whereas caspase-2 characteristically accumulates in the nucleus forming dots or filaments, the mutant enzyme is mostly localized outside and exclusively of the nucleus forming dot-like aggregates. K152A mutants can also kill transfected cells at comparable levels to the wild-type version |
647762 |
3.4.22.55 | more |
caspase prodomain-DELTA25 mutant is slightly less effective than wild-type caspase-2, inducing cell death of about 70% of transfected cells. Caspase prodomain-DELTA25 mutant cannot kill due to its impaired nuclear localization |
647762 |
3.4.22.55 | C320A |
forms a dimer only when cell are treated with DRB |
664753 |
3.4.22.55 | S157A/C320A |
nonphosphorylatable, dimerizes constitutively |
664753 |
3.4.22.55 | C303A |
inactive |
664882 |
3.4.22.55 | D152A |
pro-caspase mutant, like the wild-type, this mutant is efficiently processed between the large and the small subunit, however, it is not further processed to seperate the prodomain from the large subunit |
664882 |
3.4.22.55 | D316A |
fusion of the linker to the large subunit, toxic when expressed in yeast |
664882 |
3.4.22.55 | D316A/D330A |
abolishes auto-processing and reduces enzymatic activity dramatically, 840fold decrease in activity |
664882 |
3.4.22.55 | D330A |
fusion of the linker to the small subunit, slightly greater deleterious effect on enzyme activity than fusion to the large subunit (D316A), toxic when expressed in yeast |
664882 |
3.4.22.55 | C303A |
catalytically inactive |
665588 |