ENZYME

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.