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ENZYME

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
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
Rhea expert-curated reactions3.4.22.56
UniProtKB/Swiss-Prot
Q08DY9, CASP3_BOVINQ8MKI5, CASP3_CANLFQ8MJU1, CASP3_FELCA
P42574, CASP3_HUMANQ2PFV2, CASP3_MACFAQ60431, CASP3_MESAU
P70677, CASP3_MOUSEQ5IS54, CASP3_PANTRQ95ND5, CASP3_PIG
Q8MJC3, CASP3_RABITP55213, CASP3_RATQ5IS99, CASP3_SAIBB
P55866, CASP3_XENLA

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