A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 3.4.22.58
| Accepted Name |
|---|
| Caspase-5.
|
| Alternative Name(s) |
|---|
| CASP-5. |
| ICErel-III. |
| Ich-3. |
| ICH-3 protease. |
| 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) |
|---|
- This enzyme is part of the family of inflammatory-caspases, which
also includes caspase-1 (EC 3.4.22.36) and caspase-4 (EC 3.4.22.57)
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.
- The enzyme is able to cleave itself and the p30 caspase-1 precursor,
but is very inefficient at generating mature interleukin-1-beta
(IL-1-beta) from pro-IL-1-beta.
- Both this enzyme and caspase-4 can cleave pro-caspase-3 to release
the small subunit (p12) but not the large subunit (p17).
- Unlike caspase-4, this enzyme can be induced by lipopolysaccharide.
- Belongs to peptidase family C14.
|
| Cross-references |
|---|
| PROSITE | PDOC00864 |
| BRENDA | 3.4.22.58 |
| EC2PDB | 3.4.22.58 |
| ExplorEnz | 3.4.22.58 |
| PRIAM enzyme-specific profiles | 3.4.22.58 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.22.58 |
| IUBMB Enzyme Nomenclature | 3.4.22.58 |
| IntEnz | 3.4.22.58 |
| MEDLINE | Find literature relating to 3.4.22.58 |
| MetaCyc | 3.4.22.58 |
| UniProtKB/Swiss-Prot |
|
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UniProtKB/Swiss-Prot entries corresponding to 3.4.22.-
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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-