Caspase-3
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.56 caspase-3
Caspase-3 is an executioner caspase, together with caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60). These caspases are responsible for proteolysis of the majority of cellular polypeptides, e.g. poly(ADP-ribose) polymerase (PARP), producing the apoptotic phenotype. Procaspase-3 is activated by caspase-1, caspase-8, caspase-9 and granzyme B. It has a strict requirement for Asp at P1 and P4, with a preferred cleavage sequence Asp-Xaa-Xaa-Asp-/-, a hydrophobic residue at P2 and a hydrophilic residue at P3, although Val or Ala are also accepted. In cells it executes the demolition phase of apoptosis. It features a p17/p12 catalytic heterodimer.
Caspase-3 is an executioner caspase, together with caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60). These caspases are responsible for proteolysis of the majority of cellular polypeptides, e.g. poly(ADP-ribose) polymerase (PARP), producing the apoptotic phenotype. Procaspase-3 is activated by caspase-1, caspase-8, caspase-9 and granzyme B. It has a strict requirement for Asp at P1 and P4, with a preferred cleavage sequence Asp-Xaa-Xaa-Asp-/-, a hydrophobic residue at P2 and a hydrophilic residue at P3, although Val or Ala are also accepted. In cells it executes the demolition phase of apoptosis. It features a p17/p12 catalytic heterodimer.
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