KEGG   ENZYME: 3.4.22.58Help
Entry
EC 3.4.22.58                Enzyme                                 

Name
caspase-5;
ICErel-III;
Ich-3;
ICH-3 protease;
transcript Y;
TY;
CASP-5
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
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
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 [3,5,6]. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but is very inefficient at generating mature interleukin-1beta (IL-1beta) from pro-IL-1beta [1,4]. Both this enzyme and caspase-4 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17) [3]. Unlike caspase-4, this enzyme can be induced by lipopolysaccharide [3]. Belongs in peptidase family C14.
History
EC 3.4.22.58 created 2007
Orthology
K04395  caspase 5
Genes
HSA: 838(CASP5)
PTR: 735478(CASP5)
PPS: 100990344(CASP5)
GGO: 101136926(CASP5)
PON: 100437308(CASP5)
NLE: 100587981(CASP5)
MCC: 704964(CASP5)
MCF: 102120532(CASP5)
CSAB: 103248366
RRO: 104665270(CASP5)
RBB: 108513170(CASP5)
 » show all
Taxonomy
Reference
1  [PMID:8617266]
  Authors
Faucheu C, Blanchet AM, Collard-Dutilleul V, Lalanne JL, Diu-Hercend A.
  Title
Identification of a cysteine protease closely related to interleukin-1 beta-converting enzyme.
  Journal
Eur J Biochem 236:207-13 (1996)
DOI:10.1111/j.1432-1033.1996.t01-1-00207.x
  Sequence
[hsa:838]
Reference
2  [PMID:16465268]
  Authors
Kamada S, Funahashi Y, Tsujimoto Y.
  Title
Caspase-4 and caspase-5, members of the ICE/CED-3 family of cysteine proteases, are CrmA-inhibitable proteases.
  Journal
Cell Death Differ 4:473-8 (1997)
DOI:10.1038/sj.cdd.4400268
Reference
3  [PMID:10986288]
  Authors
Lin XY, Choi MS, Porter AG.
  Title
Expression analysis of the human caspase-1 subfamily reveals specific regulation of the CASP5 gene by lipopolysaccharide and interferon-gamma.
  Journal
J Biol Chem 275:39920-6 (2000)
DOI:10.1074/jbc.M007255200
Reference
4  [PMID:9578463]
  Authors
Fassy F, Krebs O, Rey H, Komara B, Gillard C, Capdevila C, Yea C, Faucheu C, Blanchet AM, Miossec C, Diu-Hercend A.
  Title
Enzymatic activity of two caspases related to interleukin-1beta-converting enzyme.
  Journal
Eur J Biochem 253:76-83 (1998)
DOI:10.1046/j.1432-1327.1998.2530076.x
Reference
5  [PMID:15163405]
  Authors
Martinon F, Tschopp J.
  Title
Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases.
  Journal
Cell 117:561-74 (2004)
DOI:10.1016/j.cell.2004.05.004
Reference
6  [PMID:11104820]
  Authors
Chang HY, Yang X.
  Title
Proteases for cell suicide: functions and regulation of caspases.
  Journal
Microbiol Mol Biol Rev 64:821-46 (2000)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.22.58
IUBMB Enzyme Nomenclature: 3.4.22.58
ExPASy - ENZYME nomenclature database: 3.4.22.58
BRENDA, the Enzyme Database: 3.4.22.58
CAS: 192465-11-5

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