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 |
BRENDA | 3.4.22.57 |
EC2PDB | 3.4.22.57 |
ExplorEnz | 3.4.22.57 |
PRIAM enzyme-specific profiles | 3.4.22.57 |
KEGG Ligand Database for Enzyme Nomenclature | 3.4.22.57 |
IUBMB Enzyme Nomenclature | 3.4.22.57 |
IntEnz | 3.4.22.57 |
MEDLINE | Find literature relating to 3.4.22.57 |
MetaCyc | 3.4.22.57 |
Rhea expert-curated reactions | 3.4.22.57 |
UniProtKB/Swiss-Prot |
|
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