KEGG   ENZYME: 3.4.22.36Help
Entry
EC 3.4.22.36                Enzyme                                 
Name
caspase-1;
interleukin 1beta-converting enzyme;
protease VII;
protease A;
interleukin 1beta precursor proteinase;
interleukin 1 converting enzyme;
interleukin 1beta-converting endopeptidase;
interleukin-1beta convertase;
interleukin-1beta converting enzyme;
interleukin-1beta precursor proteinase;
prointerleukin 1beta protease;
precursor interleukin-1beta converting enzyme;
pro-interleukin 1beta proteinase;
ICE
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp!
Comment
From mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) 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 [6,7]. Cleaves pro-interleukin-1beta (pro-IL-1beta) to form mature IL-1beta, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-gamma-inducing factor [6]. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mice, whereas caspase-4 enhances its activation in humans [7]. Belongs in peptidase family C14.
Orthology
K01370  
caspase 1
Genes
HSA: 
834(CASP1)
PTR: 
PPS: 
100986637(CASP1)
GGO: 
101136563(CASP1)
PON: 
100437679(CASP1)
MCC: 
706568(CASP1)
MMU: 
12362(Casp1)
RNO: 
25166(Casp1)
FCA: 
493961(CASP1)
BTA: 
514214(CASP1)
SSC: 
397319(CASP1)
ECB: 
100033888(CASP1) 100069322
MDO: 
100032592 100032596 100032610
SHR: 
100935043
OAA: 
100078458
GGA: 
395764(CASP1)
MGP: 
100549639
XLA: 
378669(casp1-b) 397719(casp1-a)
XTR: 
100491605
DRE: 
57933(caspa)
TRU: 
101080252
OLA: 
101174762
 » show all
Taxonomy
Reference
1  [PMID:1919001]
  Authors
Howard AD, Kostura MJ, Thornberry N, Ding GJ, Limjuco G, Weidner J, Salley JP, Hogquist KA, Chaplin DD, Mumford RA, et al.
  Title
IL-1-converting enzyme requires aspartic acid residues for processing of the IL-1 beta precursor at two distinct sites and does not cleave 31-kDa IL-1 alpha.
  Journal
J. Immunol. 147 (1991) 2964-9.
  Organism
Homo sapiens [GN:hsa], Mus musculus [GN:mmu]
Reference
2  [PMID:1574116]
  Authors
Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, Kostura MJ, Miller DK, Molineaux SM, Weidner JR, Aunins J, et al.
  Title
A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes.
  Journal
Nature. 356 (1992) 768-74.
  Organism
Homo sapiens [GN:hsa]
Reference
3  [PMID:7845238]
  Authors
Thornberry NA.
  Title
Interleukin-1 beta converting enzyme.
  Journal
Methods. Enzymol. 244 (1994) 615-31.
Reference
4  [PMID:8861900]
  Authors
Alnemri ES, Livingston DJ, Nicholson DW, Salvesen G, Thornberry NA, Wong WW, Yuan J.
  Title
Human ICE/CED-3 protease nomenclature.
  Journal
Cell. 87 (1996) 171.
  Organism
Homo sapiens [GN:hsa]
Reference
5  [PMID:9054418]
  Authors
Margolin N, Raybuck SA, Wilson KP, Chen W, Fox T, Gu Y, Livingston DJ.
  Title
Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases.
  Journal
J. Biol. Chem. 272 (1997) 7223-8.
  Organism
Caenorhabditis elegans [GN:cel]
Reference
6  [PMID:15163405]
  Authors
Martinon F, Tschopp J.
  Title
Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases.
  Journal
Cell. 117 (2004) 561-74.
  Organism
Homo sapiens [GN:hsa], Mus musculus [GN:mmu]
Reference
7  [PMID:11104820]
  Authors
Chang HY, Yang X.
  Title
Proteases for cell suicide: functions and regulation of caspases.
  Journal
Microbiol. Mol. Biol. Rev. 64 (2000) 821-46.
  Organism
Homo sapiens [GN:hsa], Mus musculus [GN:mmu]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
122191-40-6
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