ENZYME entry: EC 3.4.22.63

Accepted Name

caspase-10

Alternative Name(s)

apoptotic protease Mch-4

CASP-10

FAS-associated death domain protein interleukin-1beta-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 3.4.22.55), 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-kappaB 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

EC2PDB

ExplorEnz

KEGG Ligand Database for Enzyme Nomenclature

IUBMB Enzyme Nomenclature

MEDLINE

MetaCyc

Rhea expert-curated reactions

UniProtKB/Swiss-Prot

Q92851, CASPA_HUMAN

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.22.-
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