ENZYME entry: EC 3.4.22.59
Accepted Name |
Caspase-6.
|
Alternative Name(s) |
Apoptotic protease Mch-2. |
CASP-6. |
Mch2. |
Reaction catalysed |
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|- |
Comment(s) |
- Caspase-6 is an effector/executioner caspase, as are caspase-3
(EC 3.4.22.56) and caspase-7 (EC 3.4.22.60).
- 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.
- Caspase-6 can cleave its prodomain to produce mature caspase-6, which
directly activates caspase-8 (EC 3.4.22.61) and leads to cytochrome c
release from the mitochondria; the release of cytochrome c, which is
an essential component of the intrinsic apoptosis pathway.
- Can also cleave and inactivate lamins, the intermediate filament
scaffold proteins of the nuclear envelope, leading to nuclear
fragementation in the final phases of apoptosis.
- Belongs to peptidase family C14.
|
Cross-references |
PROSITE | PDOC00864 |
BRENDA | 3.4.22.59 |
EC2PDB | 3.4.22.59 |
ExplorEnz | 3.4.22.59 |
PRIAM enzyme-specific profiles | 3.4.22.59 |
KEGG Ligand Database for Enzyme Nomenclature | 3.4.22.59 |
IUBMB Enzyme Nomenclature | 3.4.22.59 |
IntEnz | 3.4.22.59 |
MEDLINE | Find literature relating to 3.4.22.59 |
MetaCyc | 3.4.22.59 |
Rhea expert-curated reactions | 3.4.22.59 |
UniProtKB/Swiss-Prot |
|
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