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 |
BRENDA | 3.4.22.60 |
EC2PDB | 3.4.22.60 |
ExplorEnz | 3.4.22.60 |
PRIAM enzyme-specific profiles | 3.4.22.60 |
KEGG Ligand Database for Enzyme Nomenclature | 3.4.22.60 |
IUBMB Enzyme Nomenclature | 3.4.22.60 |
IntEnz | 3.4.22.60 |
MEDLINE | Find literature relating to 3.4.22.60 |
MetaCyc | 3.4.22.60 |
Rhea expert-curated reactions | 3.4.22.60 |
UniProtKB/Swiss-Prot |
|
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