EC 3.4.22.60 - Caspase-7

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IntEnz Enzyme Nomenclature
EC 3.4.22.60

Names

Accepted name:
caspase-7
Other names:
CASP-7
ICE-like apoptotic protease 3
ICE-LAP3
apoptotic protease Mch-3
Mch3
CMH-1
Systematic name:
-

Reaction

Comments:

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 lead 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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00864
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Chang, H.Y. and Yang, X.
    Proteases for cell suicide: functions and regulation of caspases.
    Microbiol. Mol. Biol. Rev. 64: 821-846 (2000). [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 ed., Elsevier, London, 2004, 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: 654-666 (2006). [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: 34042-34050 (2003). [PMID: 12824163]

[EC 3.4.22.60 created 2007]