Reaction: Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp
Other name(s): CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; apoptotic protease Mch-3; Mch3; CMH-1
Comments: Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 184.108.40.206) and caspase-6 (EC 220.127.116.11) . 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 . Although a hydrophobic residue at P5 of caspase-2 (EC 18.104.22.168) 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 22.214.171.124), caspase-9 (EC 126.96.36.199) and caspase-10 (EC 188.8.131.52)]. Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits . Belongs in peptidase family C14.
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 189258-14-8
1. Chang, H.Y. and Yang, X. Proteases for cell suicide: functions and regulation of caspases. Microbiol. Mol. Biol. Rev. 64 (2000) 821-846. [PMID: 11104820]
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 edn, Elsevier, London, 2004, pp. 1298-1302.
3. Fang, B., Boross, P.I., Tozser, J. and Weber, I.T. Structural and kinetic analysis of caspase-3 reveals role for S5 binding site in substrate recognition. J. Mol. Biol. 360 (2006) 654-666. [PMID: 16781734]
4. Denault, J.B. and Salvesen, G.S. Human caspase-7 activity and regulation by its N-terminal peptide. J. Biol. Chem. 278 (2003) 34042-34050. [PMID: 12824163]