EC Number   |
Protein Variants |
Reference |
|---|
   3.4.22.62 | analysis |
optical sensor for the detection of caspase-9 in a single cell. LEHD-7-amido-4-methylcoumarin covalently attached on the nanoprobe tip of the optical sensor is cleaved during apoptosis by caspase-9 generating free 7-amino-4-methylcoumarin |
665296 |
| 3.4.22.62 | C172A |
the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme |
732880 |
| 3.4.22.62 | C239S |
the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme |
732880 |
| 3.4.22.62 | C272A |
the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme |
732880 |
| 3.4.22.62 | C272A/C287A |
the mutant enzyme shows highly reduced zinc binding compared to the wild-type enzyme |
732880 |
| 3.4.22.62 | C287A |
immunofluorescence staining of cells transiently transfected with vectors encoding caspase-9 point mutation |
697888 |
| 3.4.22.62 | C287A |
the active site mutant enzyme shows reduced zinc binding compared to the wild-type enzyme |
732880 |
| 3.4.22.62 | C287A/C239S |
the mutant enzyme shows reduced zinc binding compared to the wild-type enzyme |
732880 |
| 3.4.22.62 | C299G |
site-directed mutagenesis, the mutant displays significantly decreased proteolytic activity compared to the wild-type enzyme |
717527 |
| 3.4.22.62 | C403S |
point mutation at C403 of caspase-9 impairs its activation mediated by H2O2, interaction with APAF-1 diminished through the abolition of disulfide formation, weaker association between cytochrome c and the C403S mutant than that between cytochrome c and wild-type caspase-9 |
697186 |
