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EC 3.4.22.57 Details
EC number
3.4.22.57
Accepted name
caspase-4
Reaction
Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp┼ but also cleaves at Asp-Glu-Val-Asp┼
Other name(s)
ICErelII, ICErel-II, Ich-2, transcript X, TX, TX protease, caspase 4, CASP-4
CAS registry number
182762-08-9
Comment
This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation [3,5,6]. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but, unlike caspase-1, it is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1β [1,4]. Both this enzyme and caspase-5 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17) [3]. The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this enzyme, but more slowly [4]. 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