| Product Name |
caspase-10 |
| Example Structure |
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| Synonyms |
apoptotic protease Mch-4, C14.011, CASP10, caspase 10, caspase-10, caspase-10/b, caspase-10beta, FAS-associated death domain protein interleukin-1B-converting enzyme 2, FLICE2, ICE-like apoptotic protease 4, Mch4 |
| EC Number |
3.4.22.63 |
| CAS Registry Number |
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| Comments |
Caspase-10 is an initiator caspase, as are caspase-2 (EC?3.4.22.55), caspase-8 (EC?3.4.22.61) and caspase-9 (EC?3.4.22.62) [1]. Like caspase-8, caspase-10 contains two tandem death effector domains (DEDs) in its N-terminal prodomain, which play a role in procaspase activation [1]. The enzyme has many overlapping substrates in common with caspase-8, such as RIP (the cleavage of which impairs NF-¦ÊB survival signalling 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) [2]. 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©à 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©à to yield a p13 fragment that is not?N-myristoylated [2]. Belongs in peptidase family?C14. |
| Cofactor |
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| History |
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| Reactions |
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Leu-Gln-Thr-Asp-|-Gly. |
