Home  |  Contact

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
PROSITEPDOC00864
BRENDA3.4.22.58
EC2PDB3.4.22.58
ExplorEnz3.4.22.58
PRIAM enzyme-specific profiles3.4.22.58
KEGG Ligand Database for Enzyme Nomenclature3.4.22.58
IUBMB Enzyme Nomenclature3.4.22.58
IntEnz3.4.22.58
MEDLINEFind literature relating to 3.4.22.58
MetaCyc3.4.22.58
UniProtKB/Swiss-Prot
P51878, CASP5_HUMAN;  Q504J1, CASPB_DANRE;  

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.22.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-