A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
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 |
|---|
| PROSITE | PDOC00864 |
| 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 |
| UniProtKB/Swiss-Prot |
|
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