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-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 3.4.22.55), 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-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
PROSITEPDOC00864
BRENDA3.4.22.63
EC2PDB3.4.22.63
ExplorEnz3.4.22.63
PRIAM enzyme-specific profiles3.4.22.63
KEGG Ligand Database for Enzyme Nomenclature3.4.22.63
IUBMB Enzyme Nomenclature3.4.22.63
IntEnz3.4.22.63
MEDLINEFind literature relating to 3.4.22.63
MetaCyc3.4.22.63
UniProtKB/Swiss-Prot
Q92851, CASPA_HUMAN

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