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ENZYME

ENZYME entry: EC 3.4.22.57

Accepted Name
caspase-4
Alternative Name(s)
CASP-4
ICErelII
ICErel-II
Ich-2
Reaction catalysed
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-|-
Comment(s)
  • 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.
  • Able to cleave itself and the p30 caspase-1 precursor, but, unlike caspase-1, it is very inefficient at generating mature interleukin- 1beta (IL-1beta) from pro-IL-1beta.
  • Both this enzyme and caspase-5 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17).
  • The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this enzyme, but more slowly.
  • Belongs to peptidase family C14.
Cross-references
BRENDA3.4.22.57
EC2PDB3.4.22.57
ExplorEnz3.4.22.57
PRIAM enzyme-specific profiles3.4.22.57
KEGG Ligand Database for Enzyme Nomenclature3.4.22.57
IUBMB Enzyme Nomenclature3.4.22.57
IntEnz3.4.22.57
MEDLINEFind literature relating to 3.4.22.57
MetaCyc3.4.22.57
Rhea expert-curated reactions3.4.22.57
UniProtKB/Swiss-Prot
Q5E9C1, CASP4_BOVINP49662, CASP4_HUMAN

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