| Official Name |
|---|
| Caspase-10.
|
| Alternative Name(s) |
|---|
| Apoptotic protease Mch-4. |
| CASP-10. |
| FAS-associated death domain protein interleukin-1-beta-converting enzyme
2. |
| FLICE2. |
| ICE-like apoptotic protease 4. |
| Mch4. |
| Reaction catalysed |
|---|
| Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Leu-Gln-Thr-Asp-|-Gly |
| Comment(s) |
|---|
- Caspase-10 is an initiator caspase, as are caspase-2 (EC 3.4.22.44),
caspase-8 (EC 3.4.22.61) and caspase-9 (EC 3.4.22.62).
- Like caspase-8, it contains two tandem death effector domains (DEDs)
in its N-terminal prodomain, which play a role in procaspase
activation.
- Has many overlapping substrates in common with caspase-8, such as RIP
(the cleavage of which impairs NF-kappa-B survival signaling and
starts the cell-death process) and PAK2 (associated with some of the
morphological features of apoptosis, such as cell rounding and
apoptotic body formation).
- Bid, a Bcl2 protein, can be cleaved by caspase-3 (EC 3.4.22.56),
caspase-8 and caspase-10 at Lys-Gln-Thr-Asp-|- to yield the pro-
apoptotic p15 fragment.
- The p15 fragment is N-myristoylated and enhances cytochrome c release
from mitochondria (which initiatiates the intrinsic apoptosis
pathway).
- Bid can be further cleaved by caspase-10 and granzyme B but not by
caspase-3 and caspase-8 at Ile-Glu-Thr-Asp-|- to yield a p13 fragment
that is not N-myristoylated.
- Belongs to peptidase family C14.
|
| Cross-references |
|---|
| BRENDA | 3.4.22.63 |
| PUMA2 | 3.4.22.63 |
| PRIAM enzyme-specific profiles | 3.4.22.63 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.22.63 |
| IUBMB Enzyme Nomenclature | 3.4.22.63 |
| IntEnz | 3.4.22.63 |
| MEDLINE | Find literature relating to 3.4.22.63 |
| MetaCyc | 3.4.22.63 |
| UniProtKB/Swiss-Prot |
|
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