Information on EC 3.4.22.64 - caspase-11

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The expected taxonomic range for this enzyme is: Euarchontoglires

EC NUMBER
COMMENTARY hide
3.4.22.64
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RECOMMENDED NAME
GeneOntology No.
caspase-11
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
strict requirement for Asp at the P1 position and has a preferred cleavage sequence of (Ile/Leu/Val/Phe)-Gly-His-Asp-/-
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
216503-96-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Mus musculus C3H/An
strain C3H/An
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Mus musculus C57BL/6 X CBA
strain C57BL/6 X CBA
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-VEHD-7-amido-4-methylcoumarin + H2O
acetyl-VEHD + 7-amino-4-methylcoumarin
show the reaction diagram
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?
cationic channel subunit transient receptor potential channel 1 + H2O
?
show the reaction diagram
procaspase-1 + H2O
?
show the reaction diagram
procaspase-3 + H2O
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cationic channel subunit transient receptor potential channel 1 + H2O
?
show the reaction diagram
procaspase-1 + H2O
?
show the reaction diagram
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?
procaspase-3 + H2O
?
show the reaction diagram
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the enzyme is a critical initiator caspase responsible for the activation of caspase-3
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?
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
wedelolactone
Z-LEHD-fluoromethylketone
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cholera toxin B
additional information
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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caspase-11-deficient leukocytes are defective in migration
Manually annotated by BRENDA team
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neuroblastoma cell
Manually annotated by BRENDA team
low activity
Manually annotated by BRENDA team
additional information
no activity detected in brain
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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Flightless-I regulates the subcellular distribution of caspase-11 by promoting its localization at the cell leading edge
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Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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gene Casp11
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gene CASP11, overexpression of FLAG-tagged enzyme in HEK-293T cells, co-expression with HA-tagged cationic channel subunit transient receptor potential channel 1, i.e. TRPC1, subunits p10 and p20 of caspase-11, but not caspase recruitment domain (CARD) alone, is co-immunoprecipitated with TRPC1. FLAG-tagged caspase-11 is able to co-immunoprecipitate independently with HA-tagged TRPC1 N-terminal alone, the N-terminal domain with the transmembrane domain, and the transmembrane domain with the C-terminal domain, but not with the central transmembrane domain alone
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overexpression in Rat-1 and HeLa cells induces apoptosis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
bacterial lipopolysaccharide stimulation of caspase-11 expression in several mouse tissues, particularly in the spleen
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cytosolic infection of cells with Burkholderia species and cytyosolic mutants of Salmonella typhimurium and Legionella pneumophila trigger the enzyme
induction of caspase-11 is dependent on NF-kappaB. PARP-1 participates in the activation of caspase-11 promoter as a coactivator of NF-kappaB. Lipopolysaccharide induce the enzyme expression
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induction of procaspase-11 expression is delayed in Myd88-/- macrophages infected with DELTAFlag Salmonella typhimurium, although procaspase-11 processing itself remains intact
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ischemia induces expression in astrocytes
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Lipopolysaccharide treatment or type I IFN treatment alone does not cause caspase-11-dependent cell death
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poly(ADP-ribose) polymerase-1, PARP-1, regulates the expression of caspase-11 following lipopolysaccharide stimulation. PARP-1 is recruited to the caspase-11 promoter region containing predicted nuclear factor (NF)-kappaB-binding sites, but PARP-1 enzymatic activity is not required for the caspase-11 upregulation. PARP-1 can regulate the induction of caspase-11 at a transcriptional level. PARP-1 participates in the activation of caspase-11 promoter as a coactivator of NF-kappaB
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type I IFN signaling is sufficient to induce caspase-11 upregulation and processing. The adaptor protein TRIF upregulates procaspase-11 expression, and this upregulation is required for caspase-11 processing and activation
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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caspase-11 has a regulatory role in ethanol-induced apoptosis. Suppression of caspase-11 may be a mechanism by which Scutellariae radix (Chineses herbal medicine) exerts its cytoprotective effect