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Results 1 - 10 of 23 > >>
EC Number
Amino acid exchange
Commentary
Reference
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
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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
C320A
forms a dimer only when cell are treated with DRB
S157A/C320A
nonphosphorylatable, dimerizes constitutively
C303A
inactive
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
D316A
fusion of the linker to the large subunit, toxic when expressed in yeast
D316A/D330A
abolishes auto-processing and reduces enzymatic activity dramatically, 840fold decrease in activity
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
C303A
catalytically inactive
Results 1 - 10 of 23 > >>