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ENZYME entry: EC 3.4.22.60

Accepted Name
Caspase-7.
Alternative Name(s)
Apoptotic protease Mch-3.
CASP-7.
CMH-1.
ICE-LAP3.
ICE-like apoptotic protease 3.
Mch3.
Reaction catalysed
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-
Comment(s)
  • Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59).
  • These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which lead to the apoptotic phenotype.
  • Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect.
  • Caspase-7 is activated by the initiator caspases (caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)).
  • Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits.
  • Belongs to peptidase family C14.
Cross-references
PROSITEPDOC00864
BRENDA3.4.22.60
EC2PDB3.4.22.60
ExplorEnz3.4.22.60
PRIAM enzyme-specific profiles3.4.22.60
KEGG Ligand Database for Enzyme Nomenclature3.4.22.60
IUBMB Enzyme Nomenclature3.4.22.60
IntEnz3.4.22.60
MEDLINEFind literature relating to 3.4.22.60
MetaCyc3.4.22.60
UniProtKB/Swiss-Prot
P55210, CASP7_HUMAN;  P55214, CASP7_MESAU;  P97864, CASP7_MOUSE;  
P42573, CED3_CAEEL;  P45436, CED3_CAERE;  

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