Caspase-7
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.60 caspase-7
Caspase-7 is an executioner caspase, together with caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59), responsible for proteolysis of most cellular polypeptides, e.g. PARP, during apoptosis. A hydrophobic residue at P5 of caspase-2 and caspase-3 leads to more efficient hydrolysis. It has a strict requirement for Asp at P1 and a preferred cleavage sequence Asp-Glu-Val-Asp-/-. In cells it dismantles focal adhesions and the nuclear envelope during apoptosis. It features a p20/p11 catalytic heterodimer similar to caspase-3.
Caspase-7 is an executioner caspase, together with caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59), responsible for proteolysis of most cellular polypeptides, e.g. PARP, during apoptosis. A hydrophobic residue at P5 of caspase-2 and caspase-3 leads to more efficient hydrolysis. It has a strict requirement for Asp at P1 and a preferred cleavage sequence Asp-Glu-Val-Asp-/-. In cells it dismantles focal adhesions and the nuclear envelope during apoptosis. It features a p20/p11 catalytic heterodimer similar to caspase-3.
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