Catalytic activity:Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-. ,enzyme regulation:Inhibited by isatin sulfonamides. ,Function:Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs) . Proteolytically cleaves poly (ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death. ,PTM:Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3 , and vice versa , also occur. ,similarity:Belongs to the peptidase C14A family. ,subunit:Heterotetramer that consists of two anti-parallel arranged heterodimers , each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit. ,tissue specificity:Highly expressed in lung , skeletal muscle , liver , kidney , spleen and heart , and moderately in testis. No expression in the brain. ,
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