ENZYME entry: EC 3.4.22.56

Accepted Name
Caspase-3.
Alternative Name(s)
Apopain.
CASP-3.
CPP32.
Yama protein.
Reaction catalysed
Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
Comment(s)
  • Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60).
  • These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which leads to the apoptotic phenotype.
  • Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B.
  • Caspase-3 can activate procaspase-2 (EC 3.4.22.55).
  • Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain.
  • While Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate.
  • Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp-|- is a better substrate than Asp-Val-Ala-Asp-|-.
  • This is not the case for caspase-7.
  • Belongs to peptidase family C14.
Cross-references
PROSITEPDOC00864
BRENDA3.4.22.56
EC2PDB3.4.22.56
ExplorEnz3.4.22.56
PRIAM enzyme-specific profiles3.4.22.56
KEGG Ligand Database for Enzyme Nomenclature3.4.22.56
IUBMB Enzyme Nomenclature3.4.22.56
IntEnz3.4.22.56
MEDLINEFind literature relating to 3.4.22.56
MetaCyc3.4.22.56
UniProtKB/Swiss-Prot
Q08DY9, CASP3_BOVIN;  Q8MKI5, CASP3_CANFA;  Q8MJU1, CASP3_FELCA;  
P42574, CASP3_HUMAN;  Q2PFV2, CASP3_MACFA;  Q60431, CASP3_MESAU;  
P70677, CASP3_MOUSE;  Q5IS54, CASP3_PANTR;  Q95ND5, CASP3_PIG;  
Q8MJC3, CASP3_RABIT;  P55213, CASP3_RAT;  Q5IS99, CASP3_SAIBB;  
P55866, CASP3_XENLA;  

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