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Information on EC 3.4.22.36 - caspase-1 and Organism(s) Rattus norvegicus and UniProt Accession P43527

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.36 caspase-1
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Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P43527 not found.
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-/-
Synonyms
caspase-1, caspase 1, casp1, effector caspase, procaspase-1, interleukin-1beta-converting enzyme, interleukin-1 beta converting enzyme, interleukin-1beta converting enzyme, csp-1, il-1beta-converting enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C14.001
-
-
-
-
CASP-1
-
-
-
-
IL-1 beta converting enzyme
-
-
-
-
IL-1BC
-
-
-
-
interleukin-1 beta converting enzyme
-
-
-
-
interleukin-1-converting enzyme
-
-
interleukin-1beta-converting enzyme
-
-
-
-
p45
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
122191-40-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-Tyr-Val-Ala-Asp chloromethyl ketone
-
inhibition of caspase-1 in rat brain reduces spontaneous nonrapid eye movement sleep and nonrapid eye movement sleep enhancement induced by lipopolysaccharide
Disulfiram
-
inhibits the enzyme
N-((S,Z)-1-((S)-1-((3S)-2-ethoxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
-
good oral bioavailability (more than 50%) when administered as prodrug
N-((S,Z)-1-(2-((3S)-2-ethoxy-5-oxo-tetrahydrofuran-3-ylamino)-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
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good oral bioavailability (more than 50%) when administered as prodrug
ritonavir
-
blocks caspase-1 activation and inhibits the enzyme
additional information
-
caspase inhibition enhances neuronal survivability or protection
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
hippocampal
Manually annotated by BRENDA team
-
caspase-1 activity is required for neuronal differentiation of PC12 cells
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CASP1_RAT
402
0
45576
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
x * 45000, pro-caspase-1, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 45000, pro-caspase-1, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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ICE activity is a possible target for fighting excessive inflammatory conditions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Flaws, J.A.; Kugu, K.; Trbovich, A.M.; Desanti, A.; Tilly, K.I.; Hirshfield, A.N.; Tilly, J.L.
Interleukin-1 beta-converting enzyme-related proteases (IRPs) and mammalian cell death: dissociation of IRP-induced oligonucleosomal endonuclease activity from morphological apoptosis in granulosa cells of the ovarian follicle
Endocrinology
136
5042-5053
1995
Rattus norvegicus (P43527)
Manually annotated by BRENDA team
Keane, K.M.; Giegel, D.A.; Lipinski, W.J.; Callahan, M.J.; Shivers, B.D.
Cloning, tissue expression and regulation of rat interleukin 1 beta converting enzyme
Cytokine
7
105-110
1995
Rattus norvegicus (P43527)
Manually annotated by BRENDA team
Imeri, L.; Bianchi, S.; Opp, M.R.
Inhibition of caspase-1 in rat brain reduces spontaneous nonrapid eye movement sleep and nonrapid eye movement sleep enhancement induced by lipopolysaccharide
Am. J. Physiol. Regul. Integr. Comp. Physiol.
291
R197-R204
2006
Rattus norvegicus
Manually annotated by BRENDA team
Vaisid, T.; Kosower, N.S.; Barnoy, S.
Caspase-1 activity is required for neuronal differentiation of PC12 cells: cross-talk between the caspase and calpain systems
Biochim. Biophys. Acta
1743
223-230
2005
Rattus norvegicus
Manually annotated by BRENDA team
Wang, Y.; O'Neil, S.V.; Wos, J.A.; Oppong, K.A.; Laufersweiler, M.C.; Soper, D.L.; Ellis, C.D.; Baize, M.W.; Fancher, A.N.; Lu, W.; Suchanek, M.K.; Wang, R.L.; Schwecke, W.P.; Cruze, C.A.; Buchalova, M.; Belkin, M.; De, B.; Demuth, T.P.
Synthesis and evaluation of unsaturated caprolactams as interleukin-1beta converting enzyme (ICE) inhibitors
Bioorg. Med. Chem.
15
1311-1322
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Lu, C.; Wang, Y.; Furukawa, K.; Fu, W.; Ouyang, X.; Mattson, M.P.
Evidence that caspase-1 is a negative regulator of AMPA receptor-mediated long-term potentiation at hippocampal synapses
J. Neurochem.
97
1104-1110
2006
Rattus norvegicus
Manually annotated by BRENDA team
Juettler, E.; Bonmann, E.; Spranger, M.; Kolb-Bachofen, V.; Suschek, C.V.
A novel role of interleukin-1-converting enzyme in cytokine-mediated inducible nitric oxide synthase gene expression: Implications for neuroinflammatory diseases
Mol. Cell. Neurosci.
34
612-620
2007
Rattus norvegicus
Manually annotated by BRENDA team
Foley, K.; Kast, R.E.; Altschuler, E.L.
Ritonavir and disulfiram have potential to inhibit caspase-1 mediated inflammation and reduce neurological sequelae after minor blast exposure
Med. Hypotheses
72
150-152
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Hornung, V.; Ablasser, A.; Charrel-Dennis, M.; Bauernfeind, F.; Horvath, G.; Caffrey, D.R.; Latz, E.; Fitzgerald, K.A.
AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
Nature
458
514-518
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team