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EC 3.4.22.63 Details
EC number
3.4.22.63
Accepted name
caspase-10
Reaction
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Leu-Gln-Thr-Asp┼Gly
Other name(s)
FLICE2, Mch4, CASP-10, ICE-like apoptotic protease 4, apoptotic protease Mch-4, FAS-associated death domain protein interleukin-1β-converting enzyme 2
CAS registry number
189088-85-5
Comment
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, and these 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-κB 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┼ to yield the pro-apoptotic p15 fragment. The p15 fragment is N-myristoylated and enhances the release of cytochrome c from mitochondria (which, in turn, initiatiates the intrinsic apoptosis pathway). Bid can be further cleaved by caspase-10 and granzyme B but not by caspase-3 or caspase-8 at Ile-Glu-Thr-Asp┼ to yield a p13 fragment that is not N-myristoylated [2]. Belongs in peptidase family C14.
History
created 2007
EC Tree
2.5.1.12 created 1972, deleted 1976
2.5.1.13 created 1972, deleted 1976
2.5.1.14 created 1972, deleted 1976
2.5.1.37 created 1989, deleted 2004
2.5.1.40 created 1992, deleted 1999