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EC 3.4.22.62 Details
EC number
3.4.22.62
Accepted name
caspase-9
Reaction
Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp┼Xaa
Other name(s)
CASP-9, ICE-like apoptotic protease 6, ICE-LAP6, apoptotic protease Mch-6, apoptotic protease-activating factor 3, APAF-3
CAS registry number
180189-96-2
Comment
Caspase-9 is an initiator caspase, as are caspase -2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-10 (EC 3.4.22.63) [1]. Caspase-9 contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation [1]. An alternatively spliced version of caspase-9 also exists, caspase-9S, that inhibits apoptosis, similar to the situation found with caspase-2 [1]. Phosphorylation of caspase-9 from some species by Akt, a serine-threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo [1]. The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage [2,3]. Procaspase-3 is the enzyme’s physiological substrate [2]. Belongs in peptidase family C14.
History
created 2007
EC Tree
3.4.22.4 created 1972, deleted 1992 [EC 3.4.22.5 created 1972, incorporated 1978]
3.4.22.5 created 1972, deleted 1978
3.4.22.9 created 1972, deleted 1981
3.4.22.11 created 1976, deleted 1978 [transferred to EC 3.4.99.45, deleted 1993]
3.4.22.12 created 1978, deleted 1992
3.4.22.13 created 1978, modified 1981, deleted 1992
3.4.22.17 created 1981 [EC 3.4.24.5 created 1978, part incorporated 1989], deleted 2003
3.4.22.18 created 1981, deleted 1992
3.4.22.19 created 1989, deleted 1992
3.4.22.20 created 1989, deleted 1992
3.4.22.21 created 1989, deleted 1992
3.4.22.22 created 1989, deleted 1992
3.4.22.23 created 1989, deleted 1992