caspase-7;
CASP-7;
ICE-like apoptotic protease 3;
ICE-LAP3;
apoptotic protease Mch-3;
Mch3;
CMH-1

Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases

Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp!

Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59) [1]. 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 [2]. 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 [3]. 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 [4]. Belongs in peptidase family C14.

1  [PMID:11104820]

Chang HY, Yang X.

Proteases for cell suicide: functions and regulation of caspases.

Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.

2

Nicholson, D. and Thornberry, N.A.

Caspase-3 and caspase-7.

In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.), Handbook of Proteolytic Enzymes, 2nd ed., Elsevier, London, 2004, p. 1298-1302.

3  [PMID:16781734]

Fang B, Boross PI, Tozser J, Weber IT.

Structural and kinetic analysis of caspase-3 reveals role for s5 binding site in substrate recognition.

J. Mol. Biol. 360 (2006) 654-66.

4  [PMID:12824163]

Denault JB, Salvesen GS.

Human caspase-7 activity and regulation by its N-terminal peptide.

J. Biol. Chem. 278 (2003) 34042-50.