Activating Compound | Comment | Organism | Structure |
---|---|---|---|
APAF-1 | proteolytic activity of caspase-9 in a complex with APAF-1 is several orders of magnitude higher than that of the free enzyme. Thus, this complex functions as a holoenzyme in which caspase-9 is the catalytic subunit and APAF-1 its allosteric regulator | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
fibroblast | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
IETD-7-amido-4-trifluoromethylcoumarin + H2O | - |
Homo sapiens | IETD + 7-amino-4-trifluoromethylcoumarin | - |
? | |
pro-caspase-3 + H2O | - |
Homo sapiens | caspase-3 + ? | - |
? | |
pro-caspase-7 + H2O | - |
Homo sapiens | caspase-7 + ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | proteolytic activity of caspase-9 in a complex with APAF-1 is several orders of magnitude higher than that of the free enzyme. Thus, this complex functions as a holoenzyme in which caspase-9 is the catalytic subunit and APAF-1 its allosteric regulator | Homo sapiens |