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Information on EC 3.4.22.36 - caspase-1
for references in articles please use BRENDA:EC3.4.22.36
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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
IUBMB Comments
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-1β (pro-IL-1β) to form mature IL-1β, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-γ-inducing factor . 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 . Belongs in peptidase family C14.
The enzyme appears in viruses and cellular organisms
- 3.4.22.36
- inflammasome
-
pyroptosis
- pyrin
-
caspases
-
nod-like
- lps
- necrosis
- tnf
-
apoptosis-associated
-
speck-like
- lipopolysaccharide
- adaptor
-
pro-il-1
-
toll-like
-
card
-
domain-containing
-
nucleotide-binding
-
neuroinflammation
-
autoinflammatory
-
lps-induced
- bcl-2
-
domain-like
- thp-1
-
multiprotein
-
tunel
- microglia
-
gasdermin
-
danger
-
marrow-derived
- interleukin-18
-
leucine-rich
- cpp32
- urate
- nod2
-
damage-associated
- nigericin
- medicine
-
txnip
-
il-1ra
-
bmdms
-
pan-caspase
- hmgb1
-
gouty
- lymphopoietin
-
monosodium
-
fas-mediated
- z-vad-fmk
-
fas-associated
-
caspase-3-like
-
pathogen-associated
- z-devd-fmk
Reaction Schemes
showStrict 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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C14.001
-
-
-
-
CASP-1
Casp1
caspase-1
ICE
IL-1 beta converting enzyme
-
-
-
-
IL-1B converting enzyme
IL-1BC
-
-
-
-
interleukin-1 beta converting enzyme
-
-
-
-
interleukin-1 converting enzyme
interleukin-1B converting enzyme
interleukin-1beta-converting enzyme
-
-
-
-
p45
-
-
-
-
CASP-1
-
-
-
-
ICE
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-/-
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
122191-40-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-[[4'-(dimethylamino)phenyl]azo]-benzoic acid-YVADAPV-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
4-[[4'-(dimethylamino)phenyl]azo]-benzoic acid-YVADAPV + 5-[(2-aminoethyl)-amino]naphthalenesulfonic acid
Substrates: -
Products: -
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?
Ac-FEAD-7-amido-4-carbamoylmethylcoumarin + H2O
?
Substrates: -
Products: -
Products: -
?
Ac-FEAD-7-amido-4-carbamoylmethylcoumarin + H2O
Ac-FEAD + 7-amino-4-carbamoylmethylcoumarin
Substrates: -
Products: -
Products: -
?
Ac-LEHD-7-amido-4-methylcoumarin + H2O
Ac-LEHD + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Ac-LLSDGID-7-amido-4-carbamoylmethylcoumarin + H2O
Ac-LLSD + Gly-Ile-Asp-7-amido-4-carbamoylmethylcoumarin
Substrates: -
Products: -
Products: -
?
Ac-LSDGIDE-7-amido-4-carbamoylmethylcoumarin + H2O
Ac-Leu-Ser-Asp + GIDE-7-amido-4-carbamoylmethylcoumarin
Substrates: -
Products: -
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?
Ac-SDGIDEE-7-amido-4-carbamoylmethylcoumarin + H2O
Ac-Ser-Asp + GIDEE-7-amido-4-carbamoylmethylcoumarin
Substrates: -
Products: -
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?
Ac-SLLSDG-7-amido-4-carbamoylmethylcoumarin + H2O
Ac-SLLSD + Gly-7-amido-4-carbamoylmethylcoumarin
Substrates: -
Products: -
Products: -
?
Ac-SLLSDGI-7-amido-4-carbamoylmethylcoumarin + H2O
Ac-SLLSD + Gly-Ile-7-amido-4-carbamoylmethylcoumarin
Substrates: -
Products: -
Products: -
?
Ac-SLLSDGID-7-amido-4-carbamoylmethylcoumarin + H2O
Ac-SLLSD + Gly-Ile-Asp-7-amido-4-carbamoylmethylcoumarin
Substrates: -
Products: -
Products: -
?
Ac-SLLSDGIDE-7-amido-4-carbamoylmethylcoumarin + H2O
Ac-SLLSD + GIDE-7-amido-4-carbamoylmethylcoumarin
Substrates: -
Products: -
Products: -
?
Ac-SLLSDGIDEE-7-amido-4-carbamoylmethylcoumarin + H2O
Ac-SLLSD + GIDEE-7-amido-4-carbamoylmethylcoumarin
Substrates: -
Products: -
Products: -
?
Ac-Trp-Glu-His-Asp-7-amino-4-trifluoromethylcoumarin + H2O
?
-
Substrates: -
Products: -
Products: -
?
Ac-WEHD-7-amido-4-trifluoromethylcoumarin + H2O
?
Substrates: -
Products: -
Products: -
?
Ac-WEHD-7-amido-4-trifluoromethylcoumarin + H2O
Ac-WEHD + 7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
Ac-WQPD-7-amido-4-carbamoylmethylcoumarin + H2O
?
Substrates: -
Products: -
Products: -
?
Ac-WQPD-7-amido-4-carbamoylmethylcoumarin + H2O
Ac-WQPD + 7-amino-4-carbamoylmethylcoumarin
Substrates: -
Products: -
Products: -
?
Ac-YVAD-4-nitroanilide + H2O
Ac-YVAD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-DEVD-4-nitroanilide + H2O
acetyl-DEVD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-DQMD-4-nitroanilide + H2O
acetyl-DQMD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-FEAD-7-amido-4-methylcoumarin + H2O
acetyl-FEAD + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
acetyl-L-Leu-L-Glu-L-His-L-Asp-7-amido-4-methylcoumarin + H2O
acetyl-L-Leu-L-Glu-L-His-L-Asp + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
acetyl-L-Trp-L-Glu-L-His-L-Asp-7-amido-4-methylcoumarin + H2O
acetyl-L-Trp-L-Glu-L-His-L-Asp + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
acetyl-LEVD-4-nitroanilide + H2O
acetyl-LEVD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-VEID-4-nitroanilide + H2O
acetyl-VEID + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-VQVD-4-nitroanilide + H2O
acetyl-VQVD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-WQPD-7-amido-4-methylcoumarin + H2O
acetyl-WQPD + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
acetyl-YEVD-4-nitroanilide + H2O
acetyl-YEVD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-YEVDGW-amide + H2O
?
-
Substrates: preferred peptide substrate
Products: -
Products: -
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
carboxyfluorescein-YVAD-fluoromethylketone + H2O
?
-
Substrates: -
Products: -
Products: -
?
eukaryotic translation initiation factor 3 subunit J + H2O
?
-
Substrates: -
Products: -
Products: -
?
interferon-gamma inducing factor + H2O
?
-
Substrates: cleavage site: LESD-/-
Products: -
Products: -
?
interleukin-18 + H2O
?
-
Substrates: caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
Products: -
Products: -
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
N-acetyl-DEVD-7-amido-4-methylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-methylcoumarin
-
Substrates: preferred substrate
Products: -
Products: -
?
N-acetyl-IETD-7-amido-4-methylcoumarin + H2O
N-acetyl-IETD + 7-amino-4-methylcoumarin
-
Substrates: negligible activity
Products: -
Products: -
?
N-acetyl-LEHD-7-amido-4-methylcoumarin + H2O
N-acetyl-LEHD + 7-amino-4-methylcoumarin
-
Substrates: negligible activity
Products: -
Products: -
?
N-acetyl-WEHD-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-WEHD + 7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
p35 + H2O
100000 Da fragment + 25000 Da fragment
Substrates: cleavage at Asp87
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta
Substrates: -
Products: -
Products: -
?
pro-interleukin-33 + H2O
mature interleukin-33 + ?
-
Substrates: recombinant pro-interleukin-33 is cleaved by recombinant caspase-1 in vitro
Products: -
Products: -
?
pro-interleukin-37 + H2O
interleukin-37 propeptide
-
Substrates: caspase-1 processing at position D20 activates interleukin-37
Products: -
Products: -
?
SDGIDEE + H2O
SD + GIDEE
Substrates: the peptide is flanked by an N-terminal fluorophore and a C-terminal quencher
Products: -
Products: -
?
SLLSDGI + H2O
SLLSD + GI
Substrates: the peptide is flanked by an N-terminal fluorophore and a C-terminal quencher
Products: -
Products: -
?
SLLSDGID + H2O
SLLSDG + GID
Substrates: the peptide is flanked by an N-terminal fluorophore and a C-terminal quencher
Products: -
Products: -
?
succinyl-YVAD-7-amido-4-methylcoumarin + H2O
succinyl-YVAD + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Trp-Glu-His-Asp-p-nitroanilide + H2O
Trp-Glu-His-Asp + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-WEHD-7-amido-4-methylcoumarin + H2O
acetyl-WEHD + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
acetyl-WEHD-7-amido-4-methylcoumarin + H2O
acetyl-WEHD + 7-amino-4-methylcoumarin
-
Substrates: WEHD is the optimal tetrapeptide recognition motif
Products: -
Products: -
?
acetyl-WEHD-7-amido-4-methylcoumarin + H2O
acetyl-WEHD + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
acetyl-YVAD-4-nitroanilide + H2O
acetyl-YVAD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-YVAD-4-nitroanilide + H2O
acetyl-YVAD + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
caspase-7 + H2O
?
Substrates: gasdermin-D and caspase-7 are the key substrates downstream of NAIP5/NLRC4/CASP1/8 required for resistance to Legionella pneumophila
Products: -
Products: -
?
epidermal growth factor receptor + H2O
?
-
Substrates: cleavage during apoptosis
Products: -
Products: -
?
gasdermin D + H2O
gasdermin D amino-terminal domain + ?
Substrates: cleavage site 273LLSD/G277
Products: -
Products: -
?
gasdermin D + H2O
gasdermin D amino-terminal domain + ?
Substrates: cleavage of porcine gasdermin D by the enzyme occurs after the 276Phe-Gln-Ser-Asp279 motif
Products: -
Products: -
?
gasdermin-D + H2O
?
Substrates: gasdermin-D and caspase-7 are the key substrates downstream of NAIP5/NLRC4/CASP1/8 required for resistance to Legionella pneumophila
Products: -
Products: -
?
interleukin-1beta + H2O
?
Substrates: caspase-1 amplifies inflammation by proteolytic activation of cytokine interleukin-1beta
Products: -
Products: -
?
interleukin-1beta + H2O
?
-
Substrates: caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
Products: -
Products: -
?
interleukin-1beta + H2O
?
Substrates: caspase-1 amplifies inflammation by proteolytic activation of cytokine interleukin-1beta
Products: -
Products: -
?
LLSDGID + H2O
LLSD + GID
Substrates: the peptide is flanked by an N-terminal fluorophore and a C-terminal quencher
Products: -
Products: -
?
LSDGIDE + H2O
LSD + GIDE
Substrates: the peptide is flanked by an N-terminal fluorophore and a C-terminal quencher
Products: -
Products: -
?
MyD88 adaptor-like + H2O
?
-
Substrates: NF-kappaB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1
Products: -
Products: -
?
MyD88 adaptor-like + H2O
?
-
Substrates: caspase-1 cleaves the TLR adaptor MyD88 adaptor-like at position D198
Products: -
Products: -
?
parkin + H2O
?
-
Substrates: cleavage at Asp126-Ser127. Caspase-1 and caspase-8 dependent parkin cleavage in sporadic Parkinsons disease may play an important role in the degenerative process by initiating a vicious circle that leads to the accumulation of toxic parkin substrates, e.g. alpha-synuclein
Products: -
Products: -
?
porcine gasdermin D + H2O
?
Substrates: gasdermin D is a substrate of caspase-1 and an executioner of pyroptosus. Cleavage occurrs after the 276phenylalanine-glutamine-serine-aspartic acid279 motif of gasdermin D. The gasdermin D anamino-terminal domain generated by cleavage shows the ability to drive cell membrane rupture in eukaryotic cells
Products: -
Products: -
?
porcine gasdermin D + H2O
?
Substrates: cleavage occurrs after the 276phenylalanine-glutamine-serine-aspartic acid279 motif of gasdermin D. The gasdermin D anamino-terminal domain generated by cleavage shows the ability to drive cell membrane rupture in eukaryotic cells
Products: -
Products: -
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
Products: -
Products: -
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: virus infection by influenza A or Sendai virus induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
Products: -
Products: -
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
Substrates: -
Products: -
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?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
Substrates: cleavage to the mature interleukin-1beta
Products: -
Products: -
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
Substrates: -
Products: -
Products: -
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
Substrates: -
Products: -
Products: -
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1-dependent processing of pro-interleukin-1beta can occur in the cytosol following activation of P2X7-receptor. Structural changes preceding cell death, occurring after caspase-1 activation, promote the cellular release of interleukin-1beta
Products: -
Products: -
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 mediated maturation and secretion of IL-1beta needs a translocation competent T3SS and flagellin, but not the type III effector proteins ExoS, ExoT and ExoY. ExoS negatively regulates the Pseudomonas aeruginosa induced IL-1beta maturation by a mechanism that is dependent on its ADP ribosyltransferase activity
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?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pro-caspase-7 + H2O
caspase-7 + ?
-
Substrates: caspase-1-mediates activation of endogenous caspase-7
Products: -
Products: -
?
pro-caspase-7 + H2O
caspase-7 + ?
-
Substrates: caspase-1-mediates activation of endogenous caspase-7
Products: -
Products: -
?
pro-caspase-7 + H2O
caspase-7 + amino-terminal procaspase-7 peptide
-
Substrates: consensus caspase-7 recognition sequence DEVD, caspase-1 cleaves caspase-7 at the canonical activation sites Asp23 and Asp198, D23A/D198A double caspase-7 mutant is no substrate
Products: -
Products: -
?
pro-caspase-7 + H2O
caspase-7 + amino-terminal procaspase-7 peptide
-
Substrates: consensus caspase-7 recognition sequence DEVD, caspase-1 cleaves caspase-7 at the canonical activation sites Asp23 and Asp198, D23A/D198A double caspase-7 mutant is no substrate
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: activation
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: interleukin-18 is synthesized as a 24 kDa inactive precursor lacking a signal peptide, which is cleaved after Asp35 by caspase-1 to yield an active 8 kDa molecule
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: active caspase-1 converts inactive pro-interleukin-18 to active interleukin-18
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: activation of caspase-1 as a key event resulting in interleukin-18 production, caspase-1 is essential for interleukin-18 production in infected macrophages
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: active caspase-1 converts inactive pro-interleukin-18 to active interleukin-18
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: active caspase-1 converts inactive pro-interleukin-18 to active interleukin-18
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 propeptide
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 propeptide
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
mature interleukin-18
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
Substrates: interleukin-18 is synthesized as inactive cytoplasmic precursor that is processed into biologically activemature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
Products: -
Products: -
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
Substrates: caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
Products: -
Products: -
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
Substrates: pro-interleukin-1beta cleavage site 1 is FEAD-/-, pro-interleukin-1beta cleavage site II is YVHD-/-
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pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
Substrates: pIL-1beta is mainly processed by caspase-1, but also by caspase-3
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pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
Substrates: pIL-1beta is mainly processed by caspase-1, but also by caspase-3
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 is the enzyme responsible for the cleavage and activation of interleukin-1beta, which is a potent pro-inflammatory cytokine
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Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 activation leads to release of active interleukin-1beta from THP-1 cells, regulation, overview
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: activation
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Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: cleavage between Asp116 and Ala117, required for activation of the cytokine
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: active caspase-1 converts inactive 31 kDa pro-interleukin-1beta to 18 kDa active interleukin-1beta
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Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
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Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 is a caspase recruitment domain, CARD-containing protease required for processing of pro-interleukin-1beta in macrophages. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide, NOD2 is a NOD-like receptor, i.e. NLR. NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in MDP-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: active caspase-1 converts inactive 31 kDa pro-interleukin-1beta to 18 kDa active interleukin-1beta
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Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
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Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: active caspase-1 converts inactive 31 kDa pro-interleukin-1beta to 18 kDa active interleukin-1beta
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Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta propeptide
Substrates: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
Substrates: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta propeptide
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
Substrates: -
Products: -
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pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
Substrates: -
Products: -
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pro-interleukin-1beta + H2O
mature interleukin-1beta
-
Substrates: -
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pro-interleukin-1beta + H2O
mature interleukin-1beta
-
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: HMG-CoA reductase inhibition induces interleukin-1beta release through Rac1/PI3K/protein kinase B-dependent caspase-1 activation, overview. Caspase-1 is hyperactive in mevalonate kinase deficiency leading secretion of high levels of interleukin-1beta, regulation, overview
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pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: -
Products: -
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pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: interleukin-1beta is synthesized as inactive cytoplasmic precursor that is processed into biologically active mature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
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pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: -
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pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: caspase-1 effectively cleaves interleukin-1beta to its mature form in both heat shock and 37°C conditions
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pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
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pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: caspase-1 effectively cleaves interleukin-1beta to its mature form in both heat shock and 37°C conditions
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pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
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pro-interleukin-33 + H2O
interleukin-33 + ?
-
Substrates: activation
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pyrin + H2O
?
-
Substrates: caspase-1 cleaves pyrin at Asp330, Familial Mediterranean fever-associated mutants are cleaved more than wild-type pyrin by caspase-1. Pyrin itself regulates caspase-1 activation and interleukin-1beta production through interaction of its N-terminal PYD motif with the ASC adapterprotein, and also modulates interleukin-1beta production by interaction of its C-terminal B30.2 domain with the catalytic domains of caspase-1
Products: -
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pyrin + H2O
?
-
Substrates: recombinant substrate expressed in PT67 cells
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SLLSDG + H2O
SLLSD + Gly
Substrates: the peptide is flanked by an N-terminal fluorophore and a C-terminal quencher
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SLLSDGIDE + H2O
SLLSD + GIDE
Substrates: the peptide is flanked by an N-terminal fluorophore and a C-terminal quencher
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SLLSDGIDEE + H2O
SLLSD + GIDEE
Substrates: the peptide is flanked by an N-terminal fluorophore and a C-terminal quencher
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Products: -
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succinyl-YVAD-4-nitroanilide + H2O
succinyl-YVAD + 4-nitroaniline
Substrates: -
Products: -
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succinyl-YVAD-4-nitroanilide + H2O
succinyl-YVAD + 4-nitroaniline
-
Substrates: -
Products: -
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additional information
?
-
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Substrates: because the usage of substrate recognition subsites is an elemental distinction between caspase-1 and caspase-4, the specificity of the dog inflammatory caspase on peptides corresponding to the recognition motif is tested by using a set of internally quenched fluorogenic substrates. Like caspase-1, the dog inflammatory caspase is more influenced by the N-terminal region than by the C-terminal region
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additional information
?
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Substrates: because the usage of substrate recognition subsites is an elemental distinction between caspase-1 and caspase-4, the specificity of the dog inflammatory caspase on peptides corresponding to the recognition motif is tested by using a set of internally quenched fluorogenic substrates. Like caspase-1, the dog inflammatory caspase is more influenced by the N-terminal region than by the C-terminal region
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additional information
?
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Substrates: cell death protease essential for development. Loss of zygotic caspase-1 function in Drosophila causes larval lethality and melanotic tumors
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additional information
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-
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Substrates: the enzyme is involved in cytokine activation
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additional information
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-
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Substrates: the production of the active enzyme induces the activation of an endogenous 32000 Da (CPP32) like caspase
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additional information
?
-
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Substrates: caspase-1 is an upstream positive regulator of caspase-6-mediated cell death in primary human neurons
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additional information
?
-
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Substrates: caspase 1 activated by protease-activating factor acts upstream of mitochondria to cause release of proteins that are known to mediate apoptosis
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additional information
?
-
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Substrates: caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
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additional information
?
-
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Substrates: caspase-1 is involved in ER/Golgi-independent protein secretion. Caspase-1 activation by the inflammasome is directly linked to IL-1a secretion from activated macrophages and UV-irradiated keratinocytes. Secretion of FGF-2 also depends on caspase-1 expression and activity. Both proteins bind to caspase-1, suggesting a role of the protease as a carrier in an ER/Golgi-independent protein secretion pathway. Secretion of caspase-1 itself requires enzymatic activity, and caspase-1 inhibition therefore prevents secretion of its binding proteins
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additional information
?
-
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Substrates: anisomycin-induced activation of preformed pro-interleukin-18 is mediated by a p38 MAPK/caspase-1-dependent mechanism, whereas anisomycin-induced new synthesis of pro-interleukin-18 mRNA is mediated through p38 MAPK-dependent but caspase-1 independent mechanism
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additional information
?
-
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Substrates: the downstream signaling pathway of TLR7 and TLR8 in monocytes and dendritic cells after stimulation with specific ligands included not only the secretion of cytokines, such as TNFalpha and interleukin-1beta, but as well the activation of necessary regulating proteins like caspase-1
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additional information
?
-
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Substrates: caspase-1 is an inflammatory caspase that controls the activation and secretion of the inflammatory cytokines, interleukin-1beta and interleukin-18, active caspase-1 specifically mediates secretion of retinoic acid inducible gene-I, which is not a substrate for proteolytic cleavage by caspase-1, but caspase-1 physically interacts with full length RIG-I, although not with mutant forms lacking either the amino- or carboxyl-terminal domains
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additional information
?
-
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Substrates: caspase-1 is the prototype of the inflammatory caspases and is a component of the NALP3 inflammasome, a cytosolic multiprotein complex that mediates the processing of pro-inflammatory caspases and cytokines. The inflammasome represents the first line of defense against cellular stress and is a crucial component of innate immunity. Caspase-1 plays a central role in the mechanisms leading to labor particularly in the context of intrauterine infection/inflammation. Caspase-1 is increased in the amniotic fluid of women with preterm labor in the presence of intra-amniotic infection/inflammation
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additional information
?
-
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Substrates: caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased. Caspase-1 is activated and central to neuronal damage in disparate brain injuring events: neonatal exposure to high O2 levels, cold injury, ischemic injury, excitotoxic injury, acceleration injury, the neurotoxic recreational drug methylenedioxymethamphetamine, MDMA, and others
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additional information
?
-
-
Substrates: mevalonate kinase deficiency patients have overactive caspase-1, causing enhanced interleukin-1beta processing and subsequent inflammation in response to bacterial components
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additional information
?
-
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Substrates: inflammasomes, multiprotein complexes, regulate caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC, and playing a role in regulation of immune responses and disease pathogenesis, recognition mechanisms, inflammasome regulation system, overview. Several diseases are associated with dysregulated activation of caspase-1 and secretion of interleukin-1beta. Infection of macrophages with several Gram-negative bacteria, including Salmonella typhimurium, Legionella pneumophila and Pseudomonas aeruginosa, activates caspase-1 via NLRC4 and ASC
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additional information
?
-
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Substrates: Nod-like receptors induce assembling of the inflammasome multiprotein complexes to activate caspase-1 in response to microbial and danger signals, overview. Superoxide dismutase 1 regulates caspase-1 and endotoxic shock, a physiological posttranslational mechanism, overview. Redox-sensitive cysteine residues regulate caspase-1 to identify the redox-sensitive cysteine residues in caspase
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additional information
?
-
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Substrates: 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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additional information
?
-
-
Substrates: pyrin and caspase-1 interact in their pathway for NF-kappaB activation, mechanism and regulation, overview
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Products: -
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additional information
?
-
-
Substrates: caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
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Products: -
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additional information
?
-
-
Substrates: the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1. Proteins encoded by the nucleotide-binding domain and leucine-rich repeat, NLR, containing gene family form the central components of inflammasomes and act as intracellular sensors to detect cytosolic microbial components and danger signals, such as ATP and toxins, detailed overview. NLRs consist of three domains, besides others an N-terminal region including protein interaction domains such as the caspase recruitment domain
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additional information
?
-
-
Substrates: pro-inflammatory cytokine interleukin-18 and its activator caspase-1 are involved in acute liver failure and acute-on-chronicliver-failure
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additional information
?
-
-
Substrates: caspase-1-cleaved peptides show propensity for hydrophobic residues at P4
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additional information
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-
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Substrates: caspase-1 and caspase-9 share 100% aspartic acid in the P1 position. The structures in the cleavage sites of most caspase-1 substrates are different from that of caspase-9 substrates in the following three aspects, 1. the amino acid residues with the statistically high frequencies 2. the hydrophobic amino acid occurrence frequencies and 3. the charged amino acid occurrence frequencies, second, the amino acid pairs P1-P1' are different
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additional information
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-
-
Substrates: phenotype of aninmals deficient in caspase-1: defective lipopolysaccharide-induced secretion of interleukin-1alpha and interleukin-beta and gamma-interferon, resists endotoxic shock, thymocytes partially resistant to Fas-mediated apoptosis
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additional information
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-
Substrates: the enzyme induces apoptosis in transfected cells
Products: -
Products: -
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additional information
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-
-
Substrates: the enzyme induces apoptosis in transfected cells
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Products: -
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additional information
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-
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Substrates: caspase-1 is involved in ER/Golgi-independent protein secretion. Caspase-1 activation by the inflammasome is directly linked to IL-1a secretion from activated macrophages and UV-irradiated keratinocytes. Secretion of FGF-2 also depends on caspase-1 expression and activity. Both proteins bind to caspase-1, suggesting a role of the protease as a carrier in an ER/Golgi-independent protein secretion pathway. Secretion of caspase-1 itself requires enzymatic activity, and caspase-1 inhibition therefore prevents secretion of its binding proteins
Products: -
Products: -
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additional information
?
-
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Substrates: IRF-2 acts as a transcriptional repressor of Casp1. Absence of IRF-2 renders macrophages more sensitive to apoptotic stimuli in a caspase-1-dependent process
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additional information
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-
-
Substrates: caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
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additional information
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-
-
Substrates: functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
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additional information
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-
-
Substrates: bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine
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additional information
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-
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Substrates: caspase-1 is critical for IFN-gamma-mediated control of Anaplasma phagocytophilum infection
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additional information
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-
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Substrates: caspase-1 is important in the host response to sepsis at least in part via its ability to regulate sepsis-induced splenic cell apoptosis
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additional information
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-
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Substrates: the enzyme is involved in the cytokine metabolism, cryopyrin and caspase-1 are central to both innate immunity and to moderating lung pathology in influenza pneumonia, absence of cryopyrin and caspase-1, but not Ipaf, is associated with greater mortality, regulation, overview
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additional information
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-
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Substrates: caspase-1 mediates cell death and secretion of interleukin-1beta in native macrophages infected with Yersinia enterocolitica and Yersinia pestis, but cell death occurs independently of caspase-1 in Yersinia pestis strain KIM5, while translocation of catalytically active bacterial YopJ into macrophages is required for caspase-1 activation and cell death, regulation, overview
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additional information
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-
-
Substrates: critical involvement of pneumolysin in production of interleukin-1alpha and caspase-1-dependent cytokines in infection with Streptococcus pneumoniae in vitro
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additional information
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-
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Substrates: caspase-1 mediates resistance in murine melioidosis, caused by gram-negative rod Burkholderia pseudomallei, which can induce caspase-1-dependent cell death in macrophages. Caspase-1-dependent rapid cell death might contribute to resistance by reducing the intracellular niche for Birkholderia pseudomallei, but, in addition, caspase-1 might also have a role in controlling intracellular replication of Burkholderia pseudomallei in macrophages
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additional information
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-
-
Substrates: caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
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Products: -
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additional information
?
-
-
Substrates: the inflammasome regulatory proteins, ASC or apoptosis-associated speck-like protein containing a caspase-recruitment domain, and NLRP3 or NLR family, pyrin domain containing 3, are essential for caspase-1 activation, and also for P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome, which is, however, independent of caspase-1, overview
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Products: -
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additional information
?
-
-
Substrates: caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2
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additional information
?
-
-
Substrates: caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased
Products: -
Products: -
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additional information
?
-
-
Substrates: caspase-1 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
Products: -
Products: -
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additional information
?
-
-
Substrates: inflammasomes, multiprotein complexes, regulate caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC, and playing a role in regulation of immune responses and disease pathogenesis, recognition mechanisms, overview. Several diseases are associated with dysregulated activation of caspase-1 and secretion of interleukin-1beta
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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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Products: -
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additional information
?
-
-
Substrates: caspase-1 activation contributes to the development of nitrogen-containing bisphosphonate-associated inflammatory side effects including jaw osteomyelitis, overview
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Products: -
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additional information
?
-
-
Substrates: caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
Products: -
Products: -
?
additional information
?
-
-
Substrates: the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1. Proteins encoded by the nucleotide-binding domain and leucine-rich repeat, NLR, containing gene family form the central components of inflammasomes and act as intracellular sensors to detect cytosolic microbial components and danger signals, such as ATP and toxins, detailed overview. NLRs consist of three domains, besides others an N-terminal region including protein interaction domains such as the caspase recruitment domain
Products: -
Products: -
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additional information
?
-
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Substrates: caspase-1 activation dependent on Nalp1b, an inflammasome component, mediates cell death after pathogen infection, e.g. of dendritic cells after infection by Bacillus anthracis and lethal anthrax toxin, overview. Some dendritic cells of a certain genotype follow a caspase-1-independent way of response to infection by Bacillus anthracis, overview
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additional information
?
-
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Substrates: enzyme regulation, mechanisms of ATP-induced and caspase-1-dependent cell death and interleukin-1beta release are both regulated by zinc, overview
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additional information
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-
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Substrates: peptide substrate screening, the enzyme preferably cleaves after Asp, overview
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Products: -
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additional information
?
-
Substrates: the enzyme induces apoptosis in transfected cells
Products: -
Products: -
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additional information
?
-
-
Substrates: caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
Products: -
Products: -
?
additional information
?
-
-
Substrates: the inflammasome regulatory proteins, ASC or apoptosis-associated speck-like protein containing a caspase-recruitment domain, and NLRP3 or NLR family, pyrin domain containing 3, are essential for caspase-1 activation, and also for P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome, which is, however, independent of caspase-1, overview
Products: -
Products: -
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additional information
?
-
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Substrates: caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2
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additional information
?
-
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Substrates: caspase-1 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
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additional information
?
-
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Substrates: in brain microvascular endothelial cells and in astrocytes expression and activity of inducible nitric axide synthase exclusively depends on the endogenous availability of bioactive interleukin-1beta as inhibition of ICE activity significantly decreases promoter activity of inducible nitric axide synthase, expression and enzyme activity
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additional information
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Substrates: caspase-1 is a negative regulator of AMPA receptor-mediated long-term potentiation at hippocampal synapses
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additional information
?
-
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Substrates: caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased
Products: -
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additional information
?
-
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Substrates: 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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?
additional information
?
-
Substrates: the enzyme is able to induce apoptosis in Sf9 cells
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?
additional information
?
-
-
Substrates: the enzyme is able to induce apoptosis in Sf9 cells
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?
additional information
?
-
-
Substrates: caspase-1 is involved in this apoptosis
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Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
epidermal growth factor receptor + H2O
?
-
Substrates: cleavage during apoptosis
Products: -
Products: -
?
interferon-gamma inducing factor + H2O
?
-
Substrates: cleavage site: LESD-/-
Products: -
Products: -
?
interleukin-18 + H2O
?
-
Substrates: caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
Products: -
Products: -
?
p35 + H2O
100000 Da fragment + 25000 Da fragment
Substrates: cleavage at Asp87
Products: -
Products: -
?
parkin + H2O
?
-
Substrates: cleavage at Asp126-Ser127. Caspase-1 and caspase-8 dependent parkin cleavage in sporadic Parkinsons disease may play an important role in the degenerative process by initiating a vicious circle that leads to the accumulation of toxic parkin substrates, e.g. alpha-synuclein
Products: -
Products: -
?
porcine gasdermin D + H2O
?
Substrates: gasdermin D is a substrate of caspase-1 and an executioner of pyroptosus. Cleavage occurrs after the 276phenylalanine-glutamine-serine-aspartic acid279 motif of gasdermin D. The gasdermin D anamino-terminal domain generated by cleavage shows the ability to drive cell membrane rupture in eukaryotic cells
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta
Substrates: -
Products: -
Products: -
?
pro-interleukin-33 + H2O
mature interleukin-33 + ?
-
Substrates: recombinant pro-interleukin-33 is cleaved by recombinant caspase-1 in vitro
Products: -
Products: -
?
pro-interleukin-37 + H2O
interleukin-37 propeptide
-
Substrates: caspase-1 processing at position D20 activates interleukin-37
Products: -
Products: -
?
pyrin + H2O
?
-
Substrates: caspase-1 cleaves pyrin at Asp330, Familial Mediterranean fever-associated mutants are cleaved more than wild-type pyrin by caspase-1. Pyrin itself regulates caspase-1 activation and interleukin-1beta production through interaction of its N-terminal PYD motif with the ASC adapterprotein, and also modulates interleukin-1beta production by interaction of its C-terminal B30.2 domain with the catalytic domains of caspase-1
Products: -
Products: -
?
caspase-7 + H2O
?
Substrates: gasdermin-D and caspase-7 are the key substrates downstream of NAIP5/NLRC4/CASP1/8 required for resistance to Legionella pneumophila
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Products: -
?
gasdermin D + H2O
gasdermin D amino-terminal domain + ?
Substrates: cleavage site 273LLSD/G277
Products: -
Products: -
?
gasdermin D + H2O
gasdermin D amino-terminal domain + ?
Substrates: cleavage of porcine gasdermin D by the enzyme occurs after the 276Phe-Gln-Ser-Asp279 motif
Products: -
Products: -
?
gasdermin-D + H2O
?
Substrates: gasdermin-D and caspase-7 are the key substrates downstream of NAIP5/NLRC4/CASP1/8 required for resistance to Legionella pneumophila
Products: -
Products: -
?
interleukin-1beta + H2O
?
Substrates: caspase-1 amplifies inflammation by proteolytic activation of cytokine interleukin-1beta
Products: -
Products: -
?
interleukin-1beta + H2O
?
-
Substrates: caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
Products: -
Products: -
?
interleukin-1beta + H2O
?
Substrates: caspase-1 amplifies inflammation by proteolytic activation of cytokine interleukin-1beta
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Products: -
?
MyD88 adaptor-like + H2O
?
-
Substrates: NF-kappaB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1
Products: -
Products: -
?
MyD88 adaptor-like + H2O
?
-
Substrates: caspase-1 cleaves the TLR adaptor MyD88 adaptor-like at position D198
Products: -
Products: -
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
Products: -
Products: -
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: virus infection by influenza A or Sendai virus induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
Products: -
Products: -
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1-dependent processing of pro-interleukin-1beta can occur in the cytosol following activation of P2X7-receptor. Structural changes preceding cell death, occurring after caspase-1 activation, promote the cellular release of interleukin-1beta
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Products: -
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 mediated maturation and secretion of IL-1beta needs a translocation competent T3SS and flagellin, but not the type III effector proteins ExoS, ExoT and ExoY. ExoS negatively regulates the Pseudomonas aeruginosa induced IL-1beta maturation by a mechanism that is dependent on its ADP ribosyltransferase activity
Products: -
Products: -
?
pro-caspase-7 + H2O
caspase-7 + ?
-
Substrates: caspase-1-mediates activation of endogenous caspase-7
Products: -
Products: -
?
pro-caspase-7 + H2O
caspase-7 + ?
-
Substrates: caspase-1-mediates activation of endogenous caspase-7
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: activation
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: activation of caspase-1 as a key event resulting in interleukin-18 production, caspase-1 is essential for interleukin-18 production in infected macrophages
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 propeptide
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
interleukin-18 propeptide
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
mature interleukin-18
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
Substrates: -
Products: -
Products: -
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
Substrates: interleukin-18 is synthesized as inactive cytoplasmic precursor that is processed into biologically activemature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
Products: -
Products: -
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
Substrates: caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
Products: -
Products: -
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
Substrates: pro-interleukin-1beta cleavage site 1 is FEAD-/-, pro-interleukin-1beta cleavage site II is YVHD-/-
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Products: -
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
Substrates: pIL-1beta is mainly processed by caspase-1, but also by caspase-3
Products: -
Products: -
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
Substrates: pIL-1beta is mainly processed by caspase-1, but also by caspase-3
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 is the enzyme responsible for the cleavage and activation of interleukin-1beta, which is a potent pro-inflammatory cytokine
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 activation leads to release of active interleukin-1beta from THP-1 cells, regulation, overview
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: activation
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 is a caspase recruitment domain, CARD-containing protease required for processing of pro-interleukin-1beta in macrophages. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide, NOD2 is a NOD-like receptor, i.e. NLR. NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in MDP-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells
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Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
mature interleukin-1beta
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
mature interleukin-1beta
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: HMG-CoA reductase inhibition induces interleukin-1beta release through Rac1/PI3K/protein kinase B-dependent caspase-1 activation, overview. Caspase-1 is hyperactive in mevalonate kinase deficiency leading secretion of high levels of interleukin-1beta, regulation, overview
Products: -
Products: -
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: interleukin-1beta is synthesized as inactive cytoplasmic precursor that is processed into biologically active mature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
Products: -
Products: -
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: cell death protease essential for development. Loss of zygotic caspase-1 function in Drosophila causes larval lethality and melanotic tumors
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?
additional information
?
-
-
Substrates: the enzyme is involved in cytokine activation
Products: -
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?
additional information
?
-
-
Substrates: the production of the active enzyme induces the activation of an endogenous 32000 Da (CPP32) like caspase
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?
additional information
?
-
-
Substrates: caspase-1 is an upstream positive regulator of caspase-6-mediated cell death in primary human neurons
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase 1 activated by protease-activating factor acts upstream of mitochondria to cause release of proteins that are known to mediate apoptosis
Products: -
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?
additional information
?
-
-
Substrates: caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
Products: -
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?
additional information
?
-
-
Substrates: caspase-1 is involved in ER/Golgi-independent protein secretion. Caspase-1 activation by the inflammasome is directly linked to IL-1a secretion from activated macrophages and UV-irradiated keratinocytes. Secretion of FGF-2 also depends on caspase-1 expression and activity. Both proteins bind to caspase-1, suggesting a role of the protease as a carrier in an ER/Golgi-independent protein secretion pathway. Secretion of caspase-1 itself requires enzymatic activity, and caspase-1 inhibition therefore prevents secretion of its binding proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: anisomycin-induced activation of preformed pro-interleukin-18 is mediated by a p38 MAPK/caspase-1-dependent mechanism, whereas anisomycin-induced new synthesis of pro-interleukin-18 mRNA is mediated through p38 MAPK-dependent but caspase-1 independent mechanism
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Products: -
?
additional information
?
-
-
Substrates: the downstream signaling pathway of TLR7 and TLR8 in monocytes and dendritic cells after stimulation with specific ligands included not only the secretion of cytokines, such as TNFalpha and interleukin-1beta, but as well the activation of necessary regulating proteins like caspase-1
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Products: -
?
additional information
?
-
-
Substrates: caspase-1 is an inflammatory caspase that controls the activation and secretion of the inflammatory cytokines, interleukin-1beta and interleukin-18, active caspase-1 specifically mediates secretion of retinoic acid inducible gene-I, which is not a substrate for proteolytic cleavage by caspase-1, but caspase-1 physically interacts with full length RIG-I, although not with mutant forms lacking either the amino- or carboxyl-terminal domains
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-1 is the prototype of the inflammatory caspases and is a component of the NALP3 inflammasome, a cytosolic multiprotein complex that mediates the processing of pro-inflammatory caspases and cytokines. The inflammasome represents the first line of defense against cellular stress and is a crucial component of innate immunity. Caspase-1 plays a central role in the mechanisms leading to labor particularly in the context of intrauterine infection/inflammation. Caspase-1 is increased in the amniotic fluid of women with preterm labor in the presence of intra-amniotic infection/inflammation
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Products: -
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additional information
?
-
-
Substrates: caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased. Caspase-1 is activated and central to neuronal damage in disparate brain injuring events: neonatal exposure to high O2 levels, cold injury, ischemic injury, excitotoxic injury, acceleration injury, the neurotoxic recreational drug methylenedioxymethamphetamine, MDMA, and others
Products: -
Products: -
?
additional information
?
-
-
Substrates: mevalonate kinase deficiency patients have overactive caspase-1, causing enhanced interleukin-1beta processing and subsequent inflammation in response to bacterial components
Products: -
Products: -
?
additional information
?
-
-
Substrates: inflammasomes, multiprotein complexes, regulate caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC, and playing a role in regulation of immune responses and disease pathogenesis, recognition mechanisms, inflammasome regulation system, overview. Several diseases are associated with dysregulated activation of caspase-1 and secretion of interleukin-1beta. Infection of macrophages with several Gram-negative bacteria, including Salmonella typhimurium, Legionella pneumophila and Pseudomonas aeruginosa, activates caspase-1 via NLRC4 and ASC
Products: -
Products: -
?
additional information
?
-
-
Substrates: Nod-like receptors induce assembling of the inflammasome multiprotein complexes to activate caspase-1 in response to microbial and danger signals, overview. Superoxide dismutase 1 regulates caspase-1 and endotoxic shock, a physiological posttranslational mechanism, overview. Redox-sensitive cysteine residues regulate caspase-1 to identify the redox-sensitive cysteine residues in caspase
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: pyrin and caspase-1 interact in their pathway for NF-kappaB activation, mechanism and regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
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Products: -
?
additional information
?
-
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Substrates: the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1. Proteins encoded by the nucleotide-binding domain and leucine-rich repeat, NLR, containing gene family form the central components of inflammasomes and act as intracellular sensors to detect cytosolic microbial components and danger signals, such as ATP and toxins, detailed overview. NLRs consist of three domains, besides others an N-terminal region including protein interaction domains such as the caspase recruitment domain
Products: -
Products: -
?
additional information
?
-
-
Substrates: pro-inflammatory cytokine interleukin-18 and its activator caspase-1 are involved in acute liver failure and acute-on-chronicliver-failure
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?
additional information
?
-
-
Substrates: caspase-1-cleaved peptides show propensity for hydrophobic residues at P4
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additional information
?
-
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Substrates: phenotype of aninmals deficient in caspase-1: defective lipopolysaccharide-induced secretion of interleukin-1alpha and interleukin-beta and gamma-interferon, resists endotoxic shock, thymocytes partially resistant to Fas-mediated apoptosis
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme induces apoptosis in transfected cells
Products: -
Products: -
?
additional information
?
-
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Substrates: the enzyme induces apoptosis in transfected cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-1 is involved in ER/Golgi-independent protein secretion. Caspase-1 activation by the inflammasome is directly linked to IL-1a secretion from activated macrophages and UV-irradiated keratinocytes. Secretion of FGF-2 also depends on caspase-1 expression and activity. Both proteins bind to caspase-1, suggesting a role of the protease as a carrier in an ER/Golgi-independent protein secretion pathway. Secretion of caspase-1 itself requires enzymatic activity, and caspase-1 inhibition therefore prevents secretion of its binding proteins
Products: -
Products: -
?
additional information
?
-
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Substrates: IRF-2 acts as a transcriptional repressor of Casp1. Absence of IRF-2 renders macrophages more sensitive to apoptotic stimuli in a caspase-1-dependent process
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
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additional information
?
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Substrates: functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
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?
additional information
?
-
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Substrates: bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine
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additional information
?
-
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Substrates: caspase-1 is critical for IFN-gamma-mediated control of Anaplasma phagocytophilum infection
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?
additional information
?
-
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Substrates: caspase-1 is important in the host response to sepsis at least in part via its ability to regulate sepsis-induced splenic cell apoptosis
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?
additional information
?
-
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Substrates: the enzyme is involved in the cytokine metabolism, cryopyrin and caspase-1 are central to both innate immunity and to moderating lung pathology in influenza pneumonia, absence of cryopyrin and caspase-1, but not Ipaf, is associated with greater mortality, regulation, overview
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?
additional information
?
-
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Substrates: caspase-1 mediates cell death and secretion of interleukin-1beta in native macrophages infected with Yersinia enterocolitica and Yersinia pestis, but cell death occurs independently of caspase-1 in Yersinia pestis strain KIM5, while translocation of catalytically active bacterial YopJ into macrophages is required for caspase-1 activation and cell death, regulation, overview
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?
additional information
?
-
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Substrates: critical involvement of pneumolysin in production of interleukin-1alpha and caspase-1-dependent cytokines in infection with Streptococcus pneumoniae in vitro
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additional information
?
-
-
Substrates: caspase-1 mediates resistance in murine melioidosis, caused by gram-negative rod Burkholderia pseudomallei, which can induce caspase-1-dependent cell death in macrophages. Caspase-1-dependent rapid cell death might contribute to resistance by reducing the intracellular niche for Birkholderia pseudomallei, but, in addition, caspase-1 might also have a role in controlling intracellular replication of Burkholderia pseudomallei in macrophages
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additional information
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Substrates: caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
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additional information
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-
-
Substrates: the inflammasome regulatory proteins, ASC or apoptosis-associated speck-like protein containing a caspase-recruitment domain, and NLRP3 or NLR family, pyrin domain containing 3, are essential for caspase-1 activation, and also for P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome, which is, however, independent of caspase-1, overview
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additional information
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-
-
Substrates: caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2
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additional information
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-
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Substrates: caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased
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additional information
?
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-
Substrates: caspase-1 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
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additional information
?
-
-
Substrates: inflammasomes, multiprotein complexes, regulate caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC, and playing a role in regulation of immune responses and disease pathogenesis, recognition mechanisms, overview. Several diseases are associated with dysregulated activation of caspase-1 and secretion of interleukin-1beta
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additional information
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Substrates: 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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additional information
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Substrates: caspase-1 activation contributes to the development of nitrogen-containing bisphosphonate-associated inflammatory side effects including jaw osteomyelitis, overview
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additional information
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Substrates: caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
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additional information
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Substrates: the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1. Proteins encoded by the nucleotide-binding domain and leucine-rich repeat, NLR, containing gene family form the central components of inflammasomes and act as intracellular sensors to detect cytosolic microbial components and danger signals, such as ATP and toxins, detailed overview. NLRs consist of three domains, besides others an N-terminal region including protein interaction domains such as the caspase recruitment domain
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additional information
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Substrates: caspase-1 activation dependent on Nalp1b, an inflammasome component, mediates cell death after pathogen infection, e.g. of dendritic cells after infection by Bacillus anthracis and lethal anthrax toxin, overview. Some dendritic cells of a certain genotype follow a caspase-1-independent way of response to infection by Bacillus anthracis, overview
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additional information
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Substrates: enzyme regulation, mechanisms of ATP-induced and caspase-1-dependent cell death and interleukin-1beta release are both regulated by zinc, overview
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additional information
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Substrates: the enzyme induces apoptosis in transfected cells
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additional information
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-
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Substrates: caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
Products: -
Products: -
?
additional information
?
-
-
Substrates: the inflammasome regulatory proteins, ASC or apoptosis-associated speck-like protein containing a caspase-recruitment domain, and NLRP3 or NLR family, pyrin domain containing 3, are essential for caspase-1 activation, and also for P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome, which is, however, independent of caspase-1, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-1 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
Products: -
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?
additional information
?
-
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Substrates: in brain microvascular endothelial cells and in astrocytes expression and activity of inducible nitric axide synthase exclusively depends on the endogenous availability of bioactive interleukin-1beta as inhibition of ICE activity significantly decreases promoter activity of inducible nitric axide synthase, expression and enzyme activity
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additional information
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Substrates: caspase-1 is a negative regulator of AMPA receptor-mediated long-term potentiation at hippocampal synapses
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additional information
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Substrates: caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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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additional information
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Substrates: the enzyme is able to induce apoptosis in Sf9 cells
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additional information
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Substrates: the enzyme is able to induce apoptosis in Sf9 cells
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additional information
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Substrates: caspase-1 is involved in this apoptosis
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
high extracellular K+ levels inhibit Asc-dependent caspase-1 activation, whereas Ipaf-dependent activation was unaffected by potassium treatment
Zn2+
-
pannexin-1-dependent caspase-1 activation is regulated by zinc and induced by ATP, molecular mechanism
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1S,9S)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-9-[(isoquinolin-1-ylcarbonyl)amino]-6,10-dioxooctahydro-6H-pyridazino[1,2-a][1,2]diazepine-1-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
(3)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
(3S)-3-((6-[((4-[(6-chloropyrazin-2-yl)amino]phenyl)carbonyl)amino]-2-thiophen-2-ylhexanoyl)amino)-4-oxobutanoic acid
-
-
(3S)-3-((6-[((4-[(6-methylquinoxalin-2-yl)amino]phenyl)carbonyl)amino]-2-thiophen-2-ylhexanoyl)amino)-4-oxobutanoic acid
-
-
(3S)-3-([2-(2-fluorophenyl)-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)-4-oxobutanoic acid
-
-
(3S)-3-([2-ethyl-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)-4-oxobutanoic acid
-
-
(3S)-3-([6-(([3-methyl-4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)-4-oxobutanoic acid
-
-
(3S)-3-[([(1S,9S)-9-[(isoquinolin-1-ylcarbonyl)amino]-6,10-dioxooctahydro-6H-pyridazino[1,2-a][1,2]diazepin-1-yl]carbonyl)amino]-4-oxobutanoic acid
-
-
(3S)-3-[([(3S,6S,9aR)-6-[(isoquinolin-1-ylcarbonyl)amino]-5-oxo-2,3,5,6,9,9a-hexahydro-1H-pyrrolo[1,2-a]azepin-3-yl]carbonyl)amino]-4-oxobutanoic acid
-
-
(3S)-3-[([(4S,7S,10aS)-7-[(isoquinolin-1-ylcarbonyl)amino]-6-oxo-3,4,6,7,10,10a-hexahydro-1H-[1,4]oxazino[4,3-a]azepin-4-yl]carbonyl)amino]-4-oxobutanoic acid
-
-
(3S)-4-oxo-3-([2-phenyl-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([4-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)butanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([5-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)pentanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([6-(([4-(pyrazin-2-ylamino)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([6-(([4-(pyrazin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([7-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)heptanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-[((4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]phenyl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]-2,3-dihydropyrazin-2-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]furan-2-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)acetyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-3-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((6-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]pyridin-3-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((trans-4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]cyclohexyl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[(7-oxo-7-([4-(quinoxalin-2-ylamino)phenyl]amino)heptanoyl)amino]butanoic acid
-
-
(S)-3-((S)-2-((S)-2-(2-naphthamido)-3-methylbutanamido)-propanamido)-4-(2-hydroxy)benzylaminobutanoic acid
-
-
(S)-3-benzyloxycarbonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
1-([2-[(2,6-dimethoxyphenyl)carbonyl]hydrazino]carbonyl)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]cyclohexanecarboxamide
-
-
2,5-dichloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
-
-
3-(benzyloxycarbonylamino)-5-((2,3-dihydro-1H-inden-1-yl)methylsulfanylamido)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([(2-cyclohexylethyl)(dihydroxy)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(2-naphthalen-1-ylethyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(3-phenylpropyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(naphthalen-1-yl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(phenyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-chloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
-
-
3-[[(benzyloxy)carbonyl]amino]-5-[[(2-cyclohexylethyl)sulfonyl]amino]-4-oxopentanoic acid
-
-
5-([benzyl(dihydroxy)-lambda4-sulfanyl]amino)-3-([(benzyloxy)carbonyl]amino)-4-oxopentanoic acid
-
-
Ac-YVAD-chloromethylketone
-
inhibition of caspase-1 with Ac-YVAD-CMK prevents SphK2 cleavage
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
CA-074Me
-
the caspase-1 activation is inhibited by CA-074Me, marked inhibition at 0.05 mM
carbobenzoxy-L-valyl-L-alanyl-L-aspartyl-[O-methyl]-fluoromethylketone
-
caspase-1-specific inhibitor
carbobenzyloxy-Asp-Glu-Val-Asp-fluoromethyl ketone
-
specific to suppress the activity of Sf-caspase-1 by blocking amplification of Sfcaspase-1
carbobenzyloxy-Val-Ala-Asp-fluoromethyl ketone
-
a broad-spectrum inhibitor of initiator caspase
Cbz-Val-Asp-fluoromethylketone
-
increase in IL-1beta protein levels in a liver injury mouse model is completely prevented with the pan-caspase inhibitor demonstrating the efficacy of Cbz-Val-Asp-fluoromethylketone to block caspase-1 activity
E-64d
-
the caspase-1 activation is inhibited by E-64d, marked inhibition at 0.05 mM
flightless-I
-
inhibits caspase-1 as a pseudosubstrate. Flightless-I might function as an inhibitor of caspase-1 in living cells through a mechanism similar to that of CrmA
-
geranylgeranyl diphosphate
-
the isoprenyl intermediate of non-sterol isoprenoid biosynthesis blocks activation of caspase-1
N-((S,Z)-1-((R)-1-((3S)-2-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
-
-
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-((S)-1-((3S)-2-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
-
-
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
-
good oral bioavailability (more than 50%) when administered as prodrug
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2R)-1-carboxy-5-phenylpentan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-(benzylamino)-3-carboxypropan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-(cyclohexylamino)propan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-oxopropan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(2-fluorobenzyl)amino]propan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(2-methoxybenzyl)amino]propan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(4-hydroxybenzyl)amino]propan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[methyl(phenyl)amino]propan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[(1,3-benzodioxol-5-ylmethyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[(4-carbamoylbenzyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[benzyl(methyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
-
N-([4-(quinoxalin-2-ylamino)phenyl]carbonyl)-L-valyl-N-[(1S)-2-carboxy-1-formylethyl]-L-alaninamide
-
-
N-acetyl-L-tyrosyl-alpha-glutamyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
N-acetyl-L-tyrosylvalyl-N-[1-(carboxymethyl)-2-oxo-7-phenylheptyl]-L-alaninamide
-
-
N-carbobenzyloxy-Val-Ala-Asp-fluoromethylketone
-
i.e. Z-VAD-FMK, active-site inhibitor
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-1-benzothiophene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-3-(trifluoromethyl)benzamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-3-methoxybenzamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]isoquinoline-1-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-6-[[(phenylcarbonyl)amino]methyl]-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-6-[[(phenylsulfonyl)amino]methyl]-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(2-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(3-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(4-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-methyl-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-naphthoyl)hydrazino]carbonyl]cyclopropanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methoxybenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(4-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)-2,3-dihydro-1H-indene-2-carboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
-
-
N-[(3S)-6-(hydroxymethyl)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S,5Z)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-1,2,3,4,7,8-hexahydroazocin-3-yl]isoquinoline-1-carboxamide
-
-
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]-1-benzothiophene-2-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]benzamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]isoquinoline-1-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]naphthalene-2-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]-1-benzothiophene-2-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]-3-(trifluoromethyl)benzamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]benzamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]isoquinoline-1-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]naphthalene-2-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(benzyloxy)carbonyl]-alpha-glutamyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
N-[(benzyloxy)carbonyl]valyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
NCGC00183434
-
i.e. (S)-3-((S)-1-((S)-2-(4-amino-3-chlorobenzamido)-3,3-dimethylbutanoyl)pyrrolidine-2-carboxamido)-3-cyanopropanoic acid, competitive inhibition
NCGC00183681
-
i.e. (S)-1-((S)-2-(4-amino-3-chlorobenzamido)-3,3-dimethylbutanoyl)-N-((S)-1-cyano-2-(1H-tetrazol-5-yl)ethyl)pyrrolidine-2-carboxamide
NCGC00185682
-
i.e. 3-((S)-1-((S)-2-(4-amino-3-chlorobenzamido)-3,3-dimethylbutanoyl)pyrrolidine-2-carboxamido)-3-cyanopropanoate
serpin proteinase inhibitor 9
-
endogenous inhibitor of caspase-1 activity in human vascular smooth muscle cells
-
superoxide
-
superoxide production decreases the cellular redox potential and specifically inhibites caspase-1 by reversible oxidation and glutathionylation of the redox-sensitive cysteine residues Cys397 and Cys362
VX765
specific inhibitor; the specific caspase-1 inhibitor, alleviates lung ischemia reperfusion injury by suppressing endothelial pyroptosis and barrier dysfunction
YN-1234
-
i.e. N-2-naphthoyl-L-valyl-N-[(1S)-2-carboxy-1-formylethyl]-L-prolinamide
Z-L-Tyr-L-Val-L-Ala-L-Asp-fluoromethylketone
-
specific inhibitor for caspase-1, complete inhibition at 0.05 mM
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
irreversible active site inhibitor
IDN-6556
-
active-site inhibitor that acts through irreversible covalent modification of the catalytic cysteine residue
pralnacasan
-
VX-740, active-site inhibitor that acts through reversible covalent modification of the catalytic cysteine residue
additional information
-
a dominant-negative form of the adaptor protein ASC in THP-1 cells blocks LPS-stimulated caspase-1 activation and interleukin-1beta secretion
-
additional information
-
allosteric inhibitors in caspase-1 directly disrupt the hydrogen bond network by preventing the salt bridge between Arg286 and Glu390 from forming
-
additional information
-
caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview
-
additional information
-
caspase inhibition enhances neuronal survivability or protection
-
additional information
-
caspase-1 is not inhibited by Asp-Glu-Val-Asp-CHO, Ile-Glu-Thr-Asp-CHO, and Leu-Glu-His-Asp-CHO
-
additional information
-
caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview
-
additional information
-
heat shock inhibits caspase-1 activity while also preventing its Nalp1b or NLRP1b inflammasome-mediated or nigericin-induced activation by anthrax lethal toxin, but once caspase-1 activation is initiated, heat shock is ineffective, time dependence, overview
-
additional information
-
caspase inhibition enhances neuronal survivability or protection
-
additional information
-
caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview
-
additional information
-
caspase inhibition enhances neuronal survivability or protection
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adapter protein Asc
-
is important for caspase-1 activation during Legionella pneumophila infection, mechanism, overview. Activation of caspase-1 through Asc does not require the flagellin-sensing pathway involving the host nucleotide-binding domain and leucine-rich repeat-containing protein Ipaf, NLRC4. Asc-dependent caspase-1 activation is inhibited by high extracellular potassium levels
-
alendronate
-
a nitrogen-containing bisphosphonate, activates caspase-1, activation is inhibited by clodronate. Pretreatment of cells with alendronate augments interleukin-1beta production stimulated by Toll-like receptor ligands, augmentation is inhibited by clodronate
anthrax lethal toxin
-
rapidly activates caspase-1/interleukin-1beta-converting enzyme and induces extracellular release of interleukin-1beta and interleukin-18
-
cathepsin B
-
cathepsin B can effectively cleave and activate pro-caspase-1 in a cell-free system only at an acidic pH and in THP-1 monocytic cells after stimulation with the microbial toxin nigericin
-
Ipaf
-
i.e. host nucleotide-binding domain and leucine-rich repeatcontaining protein Ipaf or NLRC4, Ipaf-dependent activation is unaffected by potassium treatment
-
NAIP5/NLRC4 inflammasome
inflammasomes are cytosolic multi-protein complexes that detect infection or cellular damage and activate the caspase-1 protease
-
Nalp1b
-
an inflammasome component is required for caspase-1 activation, Nalp1b is a member of the NOD-like receptor family, NLR, a family of cytoplasmic proteins involved in the recognition of microbial products or danger signals. Nalp1b has a caspase recruitment domain, CARD, that allows it to interact with caspase-1
-
NOD2
-
NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in muramyl dipeptide-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells
-
protease activating factor
-
i.e. Ipaf. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf
-
simvastatin
-
blocks inhibition of caspase-1 activation, simvastatin acts synergistically with lipopolysaccharides and causes an impairment of non-sterol isoprenoid biosynthesis, the isoprenyl intermediate GGPP could block activation of caspase-1 and interleukin-1beta release, overview
thalidomide
-
thalidomide inhibits activation and activity of caspase-1 in cultured cells but not in vitro
additional information
-
TLR7 and TLR8 ligands and antiphospholipid antibodies show synergistic effects on the induction of IL-1beta and caspase-1 in monocytes and dendritic cells
-
additional information
-
transcription of caspase-1 gene is increased upon lipopolysaccharide and interferon-gamma stimulation
-
additional information
-
association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
-
additional information
-
caspase-1 is activated and central to neuronal damage in disparate brain injuring events: neonatal exposure to high O2 levels, cold injury, ischemic injury, excitotoxic injury, acceleration injury, the neurotoxic recreational drug methylenedioxymethamphetamine, MDMA, and others
-
additional information
-
activation of the Rac1/PI3K/protein kinase B pathway is required for caspase-1 activation mediating increased interleukin-1beta release
-
additional information
-
caspase-1 activation is stimulated by ATP and 120fold lipopolysaccharides
-
additional information
-
infection of macrophages with several Gram-negative bacteria, including Salmonella typhimurium, Legionella pneumophila and Pseudomonas aeruginosa, activates caspase-1 via NLRC4 and ASC, Listeria monocytogenes induces caspase-1 activation through both the NLRC4 and NLRP3 inflammasomes
-
additional information
-
caspase-1 activation is induced by ATP and lipopolysaccharides
-
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
-
additional information
-
caspase-1 activation pathways and regulation, detailed overview. Many Gram-negative bacteria, such as Salmonella typhimurium, Pseudomonas aeruginosa, Shigella flexneri, and Legionella pneumophila, can induce caspase-1 activation and rapid macrophage cell death, the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1, e.g. besides T3SS and flagellin, the host factor NLRC4 is also required for activation of caspase-1 by Salmonella typhimurium or Pseudomonas aeruginosa. Lipopolysaccharide-stimulated caspase-1 activation. Caspase-1 activation by NLRP1 does not require but is enhanced by adaptor protein ASC
-
additional information
-
Bacillus anthracis poly-gamma-D-glutamic acid capsule activates caspase-1
-
additional information
-
infection of cervical epithelial cells by Chlamydia trachomatis leads to activation of caspase-1, through a process requiring the NOD-like receptor family member NLRP3 and the inflammasome adaptor protein ASC. Elevated levels of reactive oxygen species as a result of K+ efflux are responsible for NLRP3-dependent caspase-1 activation in the infected cells
-
additional information
-
caspase-1 is activated in innate immune complexes called inflammasomes
-
additional information
-
the inflammasome activator ATP can induce the production of reactive oxygen species, which are important for caspase-1 activation
-
additional information
substrate binding increases the dimerization affinity and activity of caspase-1
-
additional information
-
association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
-
additional information
-
some members of the nucleotide-binding domain and leucine-rich-repeat-containing, NLR, gene family, including ipaf and cryopyrin, induce caspase-1 activation and the release of the interleukin-1beta and interleukin-18 through the assembly of large protein complexes called inflammasomes
-
additional information
-
caspase-1 activation in macrophages infected with Yersinia pestis KIM requires the type III secretion system effector YopJ. Yersinia pestis KIM5 strain displays an unusual ability to activate caspase-1 and kill infected macrophages compared to other Yersinia pestis and Yersinia pseudotuberculosis strains
-
additional information
-
caspase-1 is activated in macrophages stimulated with recombinant of pneumolysin but not in those stimulated with lipopolysaccharide, and the level of activation is higher in macrophages infected with wild-type Streptococcus pneumoniae serotype 2 strain D39 than in those infected with the DELTAply mutant
-
additional information
-
activation of caspase-1 in macrophages occurs independently of Nalp3 and proteasome activity
-
additional information
-
ATP induces caspase-1 expression, P2X7R-deficient macrophages exhibit no caspase-1 activation response to extracellular ATP. ATP-induced caspase-1 inflammasome activation and interleukin-1beta maturation are strictly dependent on lipopolysaccharides priming of dendritic cells before ATP stimulation
-
additional information
-
activation of caspase-1 is induced in macrophages by Listeria monocytogenes infection depending on cytolysin and listeriolysin O, after evasion from phagosome into the cytoplasm, overview
-
additional information
-
caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2 and NF-kappaB and MAPK signaling
-
additional information
-
Salmonella- and lipopolysaccharide-, and ATP-induced activation of caspase-7 by caspase-1. Caspase-1 activation involves pattern recognition receptors Ipaf and Cryopyrin, and the inflammasome adaptor ASC
-
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
-
additional information
-
infection with periodontal pathogenic bacteria, e.g. Porphyromonas gingivalis and Tannerella forsythia, leads to activation of caspase-1 in macrophages, augmented by alendronate
-
additional information
-
caspase-1 activation pathways and regulation, detailed overview. Many Gram-negative bacteria, such as Salmonella typhimurium, Pseudomonas aeruginosa, Shigella flexneri, and Legionella pneumophila, can induce caspase-1 activation and rapid macrophage cell death, the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1
-
additional information
-
nigericin-induces caspase-1 activation. Nalp1b or NLRP1b inflammasome-mediated activation of caspase-1 by anthrax lethal toxin, prevented by heat shock, overview
-
additional information
-
pannexin-1-dependent caspase-1 activation is regulated by zinc and induced by ATP, molecular mechanism
-
additional information
-
association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
-
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
-
additional information
-
the enzyme and apoptosis in SF-21 cell line are induced by the conditioned medium of the entomopathogenic fungus, Nomuraea rileyi, cell phenotype, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000134
4-[[4'-(dimethylamino)phenyl]azo]-benzoic acid-YVADAPV-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
pH 7.5
0.022
Ac-LLSDGID-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.115
Ac-LSDGIDE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.038
Ac-SDGIDEE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.087
Ac-SLLSDG-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.052
Ac-SLLSDGI-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.049
Ac-SLLSDGID-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.038
Ac-SLLSDGIDE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.047
Ac-SLLSDGIDEE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.021
acetyl-FEAD-7-amido-4-methylcoumarin
pH 7.2, 37°C, recombinant enzyme
-
0.016
acetyl-WQPD-7-amido-4-methylcoumarin
pH 7.2, 37°C, recombinant enzyme
-
additional information
additional information
-
wild-type and mutant enzyme kinetics, caspase-1 shows positive cooperativity, a network of 21 hydrogen bonds from nine side chains connecting the active and allosteric sites change partners when going between the on-state and the off-state, an allosteric circuit promotes site-to-site coupling. Arg286 and Glu390, which form a salt bridge, have major effects, causing 100 to 200fold reductions in catalytic efficiency, kcat/Km. Two neighbors, Ser332 and Ser339, have minor effects, causing 4 to 7fold reductions, overview
-
0.021
Ac-FEAD-7-amido-4-carbamoylmethylcoumarin
at pH 7.2 and 37°C
-
0.038
Ac-WEHD-7-amido-4-trifluoromethylcoumarin
at pH 7.2 and 37°C
-
0.0115
Ac-WQPD-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.016
Ac-WQPD-7-amido-4-carbamoylmethylcoumarin
at pH 7.2 and 37°C
-
0.038
acetyl-WEHD-7-amido-4-methylcoumarin
pH 7.2, 37°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.41
4-[[4'-(dimethylamino)phenyl]azo]-benzoic acid-YVADAPV-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
pH 7.5
4.93
Ac-LLSDGID-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.3
Ac-LSDGIDE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.02
Ac-SDGIDEE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
1.06
Ac-SLLSDG-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
3.75
Ac-SLLSDGI-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
2.23
Ac-SLLSDGID-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
3
Ac-SLLSDGIDE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
2.72
Ac-SLLSDGIDEE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
1.22
acetyl-FEAD-7-amido-4-methylcoumarin
pH 7.2, 37°C, recombinant enzyme
-
2.96
acetyl-WQPD-7-amido-4-methylcoumarin
pH 7.2, 37°C, recombinant enzyme
-
1.22
Ac-FEAD-7-amido-4-carbamoylmethylcoumarin
at pH 7.2 and 37°C
-
8.87
Ac-WEHD-7-amido-4-trifluoromethylcoumarin
at pH 7.2 and 37°C
-
2.96
Ac-WQPD-7-amido-4-carbamoylmethylcoumarin
at pH 7.2 and 37°C
-
8.87
acetyl-WEHD-7-amido-4-methylcoumarin
pH 7.2, 37°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
226
Ac-LLSDGID-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
2.6
Ac-LSDGIDE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
0.77
Ac-SDGIDEE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
74.4
Ac-SLLSDGI-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
44.5
Ac-SLLSDGID-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
79.6
Ac-SLLSDGIDE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
58.4
Ac-SLLSDGIDEE-7-amido-4-carbamoylmethylcoumarin
pH 7.2, 37°C
-
58.1
acetyl-FEAD-7-amido-4-methylcoumarin
pH 7.2, 37°C, recombinant enzyme
-
233.42
acetyl-WEHD-7-amido-4-methylcoumarin
pH 7.2, 37°C, recombinant enzyme
185
acetyl-WQPD-7-amido-4-methylcoumarin
pH 7.2, 37°C, recombinant enzyme
-
57
Ac-FEAD-7-amido-4-carbamoylmethylcoumarin
at pH 7.2 and 37°C
-
233
Ac-WEHD-7-amido-4-trifluoromethylcoumarin
at pH 7.2 and 37°C
-
180
Ac-WQPD-7-amido-4-carbamoylmethylcoumarin
at pH 7.2 and 37°C
-
45.51
SLLSDGID
pH 7.2, 37°C, recombinant enzyme, calculated by BRENDA
-
additional information
additional information
-
kcat/Km of the dog inflammatory caspase for internally quenched substrates surrounding the gasdermin D cleavage site motif sequence, overview
-
additional information
additional information
kcat/Km of the dog inflammatory caspase for internally quenched substrates surrounding the gasdermin D cleavage site motif sequence, overview
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000054
(3S)-3-((6-[((4-[(6-chloropyrazin-2-yl)amino]phenyl)carbonyl)amino]-2-thiophen-2-ylhexanoyl)amino)-4-oxobutanoic acid
-
-
0.000005
(3S)-3-((6-[((4-[(6-methylquinoxalin-2-yl)amino]phenyl)carbonyl)amino]-2-thiophen-2-ylhexanoyl)amino)-4-oxobutanoic acid
-
-
0.000008
(3S)-3-([2-(2-fluorophenyl)-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)-4-oxobutanoic acid
-
-
0.000016
(3S)-3-([2-ethyl-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)-4-oxobutanoic acid
-
-
0.000004
(3S)-3-([6-(([3-methyl-4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)-4-oxobutanoic acid
-
-
0.000005
(3S)-4-oxo-3-([2-phenyl-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.0052
(3S)-4-oxo-3-([4-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)butanoyl]amino)butanoic acid
-
-
0.0028
(3S)-4-oxo-3-([5-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)pentanoyl]amino)butanoic acid
-
-
0.0001
(3S)-4-oxo-3-([6-(([4-(pyrazin-2-ylamino)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
0.037
(3S)-4-oxo-3-([6-(([4-(pyrazin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.00019
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.000043 - 0.00032
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
0.0024
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.000005 - 0.0026
(3S)-4-oxo-3-([7-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)heptanoyl]amino)butanoic acid
0.0001
(3S)-4-oxo-3-[((4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]phenyl)carbonyl)amino]butanoic acid
-
-
0.00026
(3S)-4-oxo-3-[((4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)carbonyl)amino]butanoic acid
-
-
0.001
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]-2,3-dihydropyrazin-2-yl)carbonyl)amino]butanoic acid
-
-
0.0021
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]furan-2-yl)carbonyl)amino]butanoic acid
-
-
0.00012
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)acetyl)amino]butanoic acid
-
-
0.000035
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)carbonyl)amino]butanoic acid
-
-
0.00012
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-3-yl)carbonyl)amino]butanoic acid
-
-
0.000005
(3S)-4-oxo-3-[((6-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]pyridin-3-yl)carbonyl)amino]butanoic acid
-
-
0.00195
(3S)-4-oxo-3-[((trans-4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]cyclohexyl)carbonyl)amino]butanoic acid
-
-
0.0021
(3S)-4-oxo-3-[(7-oxo-7-([4-(quinoxalin-2-ylamino)phenyl]amino)heptanoyl)amino]butanoic acid
-
-
0.000047
(S)-3-((S)-2-((S)-2-(2-naphthamido)-3-methylbutanamido)-propanamido)-4-(2-hydroxy)benzylaminobutanoic acid
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.024
(S)-3-benzenesulfonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
0.025
(S)-3-benzyloxycarbonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
0.065
3-([(benzyloxy)carbonyl]amino)-5-([(2,3-dihydro-1H-inden-1-ylmethyl)(dihydroxy)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.016
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(2-naphthalen-1-ylethyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.011
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.0345
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(3-phenylpropyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.022
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(naphthalen-1-yl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.037
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(phenyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.033
3-[[(benzyloxy)carbonyl]amino]-5-[[(2-cyclohexylethyl)sulfonyl]amino]-4-oxopentanoic acid
-
-
0.018
5-([benzyl(dihydroxy)-lambda4-sulfanyl]amino)-3-([(benzyloxy)carbonyl]amino)-4-oxopentanoic acid
-
-
0.05
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2R)-1-carboxy-5-phenylpentan-2-yl]-L-alaninamide
-
IC50 above 0.05 mM, in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.0006
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-(benzylamino)-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000945
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-(cyclohexylamino)propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.0012
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(2-fluorobenzyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000965
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(2-methoxybenzyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00137
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(4-hydroxybenzyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000128
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[methyl(phenyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00029
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[(1,3-benzodioxol-5-ylmethyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00182
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[(4-carbamoylbenzyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00189
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[benzyl(methyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000004
N-([4-(quinoxalin-2-ylamino)phenyl]carbonyl)-L-valyl-N-[(1S)-2-carboxy-1-formylethyl]-L-alaninamide
-
-
0.000004
N-acetyl-L-tyrosyl-alpha-glutamyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
0.000014
N-acetyl-L-tyrosylvalyl-N-[1-(carboxymethyl)-2-oxo-7-phenylheptyl]-L-alaninamide
-
-
0.0000239
N-[(benzyloxy)carbonyl]-alpha-glutamyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
0.000004
N-[(benzyloxy)carbonyl]valyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
0.0000004
NCGC00183434
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
additional information
additional information
-
the Ki-value for acetyl-IETD-aldehyde is below 6 nM and the Ki-value for acetyl-AEVD-aldehyde is below 12 nM
-
0.000043
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
0.00032
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
0.000005
(3S)-4-oxo-3-([7-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)heptanoyl]amino)butanoic acid
-
-
0.0026
(3S)-4-oxo-3-([7-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)heptanoyl]amino)butanoic acid
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000036
(1S,9S)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-9-[(isoquinolin-1-ylcarbonyl)amino]-6,10-dioxooctahydro-6H-pyridazino[1,2-a][1,2]diazepine-1-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.000004
(3S)-3-[([(1S,9S)-9-[(isoquinolin-1-ylcarbonyl)amino]-6,10-dioxooctahydro-6H-pyridazino[1,2-a][1,2]diazepin-1-yl]carbonyl)amino]-4-oxobutanoic acid
Homo sapiens
-
-
0.000004
(3S)-3-[([(3S,6S,9aR)-6-[(isoquinolin-1-ylcarbonyl)amino]-5-oxo-2,3,5,6,9,9a-hexahydro-1H-pyrrolo[1,2-a]azepin-3-yl]carbonyl)amino]-4-oxobutanoic acid
Homo sapiens
-
-
0.000003
(3S)-3-[([(4S,7S,10aS)-7-[(isoquinolin-1-ylcarbonyl)amino]-6-oxo-3,4,6,7,10,10a-hexahydro-1H-[1,4]oxazino[4,3-a]azepin-4-yl]carbonyl)amino]-4-oxobutanoic acid
Homo sapiens
-
-
0.0007
1-([2-[(2,6-dimethoxyphenyl)carbonyl]hydrazino]carbonyl)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000007 - 0.000015
2,5-dichloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
0.000008 - 0.000029
3-chloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
0.000015
acetyl-L-Leu-L-Glu-L-His-L-Asp-CHO
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.0000216
L-Tyr-L-Val-L-Ala-L-Asp-CN
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.000001
N-((S,Z)-1-((R)-1-((3S)-2-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
Homo sapiens
-
-
0.000013
N-((S,Z)-1-((S)-1-((3S)-2-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
Homo sapiens
-
-
0.00002
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-1-benzothiophene-2-carboxamide
Homo sapiens
-
-
0.000011
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-3-(trifluoromethyl)benzamide
Homo sapiens
-
-
0.000053
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-3-methoxybenzamide
Homo sapiens
-
-
0.000168
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
0.000027
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]isoquinoline-1-carboxamide
Homo sapiens
-
-
0.000014
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000002
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-6-[[(phenylcarbonyl)amino]methyl]-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000003
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-6-[[(phenylsulfonyl)amino]methyl]-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000002
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(2-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000001
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(3-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000001
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(4-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000019
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-methyl-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.00024
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
Homo sapiens
-
-
0.0002
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
Homo sapiens
-
-
0.00043
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
Homo sapiens
-
-
0.00049
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
Homo sapiens
-
-
0.00031
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.0029
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-naphthoyl)hydrazino]carbonyl]cyclopropanecarboxamide
Homo sapiens
-
-
0.00026
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methoxybenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00015
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00058
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(4-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00005
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00005
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.0004
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
Homo sapiens
-
-
0.00024
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00009
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.00015
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
Homo sapiens
-
-
0.00043
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)-2,3-dihydro-1H-indene-2-carboxamide
Homo sapiens
-
-
0.00004
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
Homo sapiens
-
-
0.00003
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
Homo sapiens
-
-
0.000022
N-[(3S)-6-(hydroxymethyl)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000077
N-[(3S,5Z)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-1,2,3,4,7,8-hexahydroazocin-3-yl]isoquinoline-1-carboxamide
Homo sapiens
-
-
0.00032
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]-1-benzothiophene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.0023
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]benzamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00013
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]isoquinoline-1-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00015
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]naphthalene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00008
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]-1-benzothiophene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
9
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]-3-(trifluoromethyl)benzamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00035
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]benzamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00007
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]isoquinoline-1-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00003
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]naphthalene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.000000023
NCGC00183434
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.00000258
NCGC00183681
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.0000434
NCGC00185682
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.000000204
VRT-043198
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.000007
2,5-dichloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
0.000015
2,5-dichloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
0.000008
3-chloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
0.000029
3-chloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
648078, 648080, 667948, 667986, 668193, 668568, 678593, 678637, 678638, 679075, 679079, 679632, 681250, 691461, 696933, 697180, 697566, 698216, 699341, 699419, 699547, 699610, 699968, 700240, 700362, 700365, 700393, 707154, 707323, 707393, 708128, 708251, 708272, 708722, 709056, 709153, 709224, 709359, 709475
-
-
brenda
-
668930, 669224, 670356, 677504, 679079, 679097, 679121, 679246, 679440, 681006, 681017, 681030, 681202, 681208, 681799, 682588, 697180, 697196, 698215, 698245, 699968, 700362, 700393, 700983, 701307, 707321, 707322, 708598, 708709, 708712, 709269, 709361, 717941, 718427, 731041, 731863, 732262, 732557, 732829, 769457
-
-
brenda
mutant mouse bearing amino acid differences in Naip5, one of the NOD-like receptors (NLRs), one of the adaptor proteins for caspase-1 activation
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
increased enzyme content during pregnancy, women with spontaneous labor at term have a higher median caspase-1 amniotic fluid concentration than women at term without labor
brenda
-
functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
brenda
of feeding and wandering larvae. Expression of Hearm caspase-1 in the haemocytes appears to be correlated with the pulse of ecdysone, and it is up-regulated by ecdysone agonist RH-2485, implying that Hearm caspase-1 activation is regulated by ecdysone
brenda
-
caspase-1 gene is expressed in 1 day post-hatching larvae and its mRNA levels increases throughout development
brenda
-
high activity in from peripheral blood of mevalonate kinase deficiency patients
brenda
-
caspase-1 activity is required for neuronal differentiation of PC12 cells
brenda
-
bacterial infection leads to a decrease in the mRNA levels of caspase-1
brenda
-
high activity. Bacterial infection leads to a decrease in the mRNA levels of caspase-1
brenda
additional information
-
acute coronary syndromes is related to increased concentration of systemic soluble ICE. Patients with myocardial infarction demonstrate heightened systemic levels of ICE as compared to patients with stable angina and patients with unstable angina
brenda
-
bacterial infection leads to a decrease in the mRNA levels of caspase-1
brenda
-
inhibition of caspase-1 in rat brain reduces spontaneous nonrapid eye movement sleep and nonrapid eye movement sleep enhancement induced by lipopolysaccharide
brenda
-
high activity. Bacterial infection leads to a decrease in the mRNA levels of caspase-1
brenda
-
Salmonella enterica serovar typhimurium invades host macrophages and induces a unique caspase-1-dependent pathway of cell death termed pyroptosis, which is activated during bacterial infection in vivo. DNA cleavage during pyroptosis results from caspase-1-stimulated nuclease activity. Membrane pores between 1.1 and 2.4 nm in diameter form during pyroptosis of host cells and cause swelling and osmotic lysis. Pore formation requires host cell actin cytoskeleton rearrangements and caspase-1 activity, as well as the bacterial type III secretion system
brenda
-
bacterial infection leads to a decrease in the mRNA levels of caspase-1
brenda
-
low activity. Bacterial infection leads to a decrease in the mRNA levels of caspase-1
brenda
-
inactive 45000 Da proform of caspase-1 is basally expressed in macrophages, virus infection induces the cleavage of procaspase into the mature 20000 Da form
brenda
-
bone marrow-derived macrophages, wild-type and superoxide dismutase-deficient
brenda
-
IFN regulatory factor IRF-2(-/-) macrophages exhibit increased basal and gliotoxin-induced caspase-1 mRNA expression and enhanced caspase-1 activity
brenda
-
caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
brenda
-
the Gram-negative bacterium Shigella flexneri triggers pro-inflammatory apoptotic cell death in macrophages, which is crucial for the onset of an acute inflammatory diarrhoea termed bacillary dysentery. The Mxi-Spa type III secretion system promotes bacterial uptake and escape into the cytoplasm, where, dependent on the translocator/effector protein IpaB, caspase-1 and its substrate IL-1b are activated
brenda
-
bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine
brenda
-
both the active and the precursor domains of caspase-1are localized in the cytoplasmatic matrix and on the cell surface
brenda
-
primary neuron, caspase-1 is an upstream positive regulator of caspase-6-mediated cell death in primary human neurons
brenda
-
caspase-1 is increased in lesional psoriatic skin capared with non-lesional psoriatic skin
brenda
-
bacterial infection leads to a decrease in the mRNA levels of caspase-1
brenda
-
quantification of caspase-1 p20 subunit levels in culture supernatants of THP-1 cells
brenda
additional information
-
caspase-1 activity is not detected in Jurkat cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
caspase-1 is responsible for the pathogenesis of I/R-induced lung injury as a consequence of mediating endothelial pyroptosis and causing barrier dysfunction. The specific caspase-1 inhibitor, alleviates lung ischemia reperfusion injury by suppressing endothelial pyroptosis and barrier dysfunction
evolution
malfunction
metabolism
physiological function
additional information
evolution
an ancient inflammatory locus reveals switch to caspase-1 specificity on a caspase-4 scaffold. Caspase-1 is lost in a Carnivora ancestor, perhaps upon a selective pressure for which the generation of biologically active IL-1beta by caspase-1 is detrimental. Carnivora possess an inflammatory caspase with caspase-1 catalytic function placed on a caspase-4 scaffold
evolution
modern mammals of the order Carnivora lack the caspase-1 catalytic domain but express an unusual version of caspase-4 that can activate both gasdermin D and IL-1beta, evolutionary origin of this caspase, overview. Ancestral sequence reconstruction of an inflammatory caspase of a Carnivora ancestor and expression of the catalytic domain of this putative ancestor in Escherichia coli, comparison of its substrate specificity on synthetic and protein substrates to extant caspases. The enzyme activates gasdermin D but has reduced ability to activate IL-1beta. The dog genome contains a single caspase-1 and caspase-4-like gene. This gene encodes a protein called hybrid caspase-1/caspase-4 or hybrid inflammatory caspase, which contains a caspase-1 CARD followed by a caspase-4 CARD and catalytic domain. Caspase-4-like protease that lacked the ability to convert pro-IL-1beta gave rise to the inflammatory caspase of extant Carnivora, evolutionary process that generated the caspase-1 function on the caspase-4 catalytic domain scaffold, overview
evolution
an ancient inflammatory locus reveals switch to caspase-1 specificity on a caspase-4 scaffold. Caspase-1 is lost in a Carnivora ancestor, perhaps upon a selective pressure for which the generation of biologically active IL-1beta by caspase-1 is detrimental. Carnivora possess an inflammatory caspase with caspase-1 catalytic function placed on a caspase-4 scaffold
evolution
an ancient inflammatory locus reveals switch to caspase-1 specificity on a caspase-4 scaffold. Caspase-1 is lost in a Carnivora ancestor, perhaps upon a selective pressure for which the generation of biologically active IL-1beta by caspase-1 is detrimental. Carnivora possess an inflammatory caspase with caspase-1 catalytic function placed on a caspase-4 scaffold
malfunction
gene silencing of caspase-1 or inhibition of caspase-1 activity leads to reduction in dengue virus-induced apoptosis with minimal effect on virus replication
malfunction
-
caspase 1 deficiency does not affect neutrophil-dominated joint inflammation, whereas in chronic arthritis, the lack of caspase 1 results in reduced joint inflammation and cartilage destruction
malfunction
-
infection with Mycobacterium leprae induces high levels of TNF-alpha production and NF-kappaB activation in macrophages of A/J mice (mutant mouse bearing amino acid differences in Naip5, one of the NOD-like receptors (NLRs), one of the adaptor proteins for caspase-1 activation) and C57BL/6 macrophages. Caspase-1 activation and IL-1beta secretion are also induced in both macrophages. Macrophages from A/J mice exhibit reduced caspase-1 activation and IL-1beta secretion compared to C57BL/6 macrophages
malfunction
-
release of truncated SphK2 into the supernatant is attenuated in caspase-1 knockdown cells
malfunction
-
apoptosis is triggered upon bacterial infection in primary murine bone marrow macrophages lacking caspase-1
malfunction
decreased enzymatic activity of caspase-1 is compatible with normal life and does not prevent moderate and severe autoinflammation
malfunction
overexpression of caspase-1 inhibits NF-kappaB activation and promotes P53 activation in grouper spleen cells
malfunction
enzyme-deficient mice are partially susceptible to Legionella pneumophila
metabolism
-
caspase-1 is required for nuclear translocation of intracellular interleukin-37 and for secretion of mature interleukin-37
metabolism
pyroptosis is a mechanism of inflammatory cell death mediated by the activation of the prolytic protein gasdermin D through caspase-1, caspase-4, and caspase-5 in human, and caspase-1 and caspase-11 in mouse. Dog inflammatory caspase shows caspase-1-like specificity
physiological function
-
NACHT, LRR, and pyrin domain-containing protein 3 inflammasome is constitutively assembled and activated with cleavage of caspase-1 in human melanoma cells
physiological function
-
in monocytes and macrophages, caspase-1 is involved in processing and secretion of pro-inflammatory cytokines such as interleukin-1beta, while in epithelial cells caspase-1 enhances lipid metabolism. In cervical epithelial cells, caspase-1 activation is required for optimal growth of the intracellular chlamydiae
physiological function
-
caspase-1-mediated MyD88 adaptor-like cleavage is not required for MyD88 adaptor-like interaction with Toll-like receptor 4 or MyD88, nor for MyD88 adaptor-like induced NF-kappaB activation
physiological function
-
the role of caspase-1 in inducing the CD4+ T cell activity increases with interleukin-18 rather than CD8+ suppressor cell activity. There is a selective deletion of T lymphocytes mediated by caspase-1 via interleukin-18
physiological function
-
caspase-1 is dispensable for interleukin-33 release by macrophages
physiological function
-
caspase-1 mediates cell death, monocytes are capable of delivering a cell death message which depends upon the release of microvesicles containing functional caspase-1. Encapsulation is necessary for exogenous caspase-1 induced cell death
physiological function
-
the production of interleukin-1beta by neutrophils and mast cells is not exclusively dependent on caspase 1, and other proteases can compensate for the loss of caspase 1 in vivo
physiological function
-
caspase 1 is a major regulator of the inflammation response
physiological function
-
caspase-1 is mainly involved in cytokine maturation, leading to an inflammatory response
physiological function
-
during cell death, sphingosine kinase 2 (SphK2) is cleaved at its N-terminus in a caspase-1-dependent manner. A truncated but enzymatically active fragment of SphK2 is released from cells
physiological function
-
lysosome exocytosis is a conserved caspase-1-dependent feature of pyroptosis. Caspase-1 activation leads to increased membrane permeability and an influx of calcium, which results in fusion of lysosomes with the cell surface and release of lysosomal contents. Secretion of processed IL-1beta and IL-18 in macrophages undergoing pyroptosis occurs independently of lysosome exocytosis. Multiple stimuli, acting through a diverse set of NLR proteins, lead to two conserved caspase-1-dependent secretion events: the release of processed inflammatory cytokines and lysosome-mediated release of antimicrobial host factors and degraded microbial products
physiological function
-
caspase-1 activity is required for UVB-induced apoptosis of human keratinocytes and therefore plays a protective role of the protease in UVB-induced skin cancer development
physiological function
-
upon Salmonella infection, inflammasome-mediated caspase-1 activity is required to bypass apoptosis in favor of pro-inflammatory pyroptotic cell death
physiological function
-
lysosomal swelling and mitochondrial impairment contribute to caspase-1 activation and to the consequent interleukin-1beta release
physiological function
-
caspase-1 is one of the main components of the NALP3 inflammasome
physiological function
-
caspase-1 activity affects AIM2 speck formation/stability through a negative feedback loop during Francisella infection
physiological function
caspase-1 is a proinflammatory enzyme that plays pivotal roles in innate immunity and many inflammatory conditions such as periodic fever syndromes and gout
physiological function
-
human procaspase-1 variants with decreased enzymatic activity are associated with febrile episodes and may contribute to inflammation via receptor interacting protein kinase 2 and nuclear factor-kappaB signaling
physiological function
-
the processing and release of the regulatory caspase-1 substrate interleukin-18 counteracts the proinflammatory activities of another caspase-1 substrate, interleukin-1beta, thereby balancing control of the Helicobacter infection with the prevention of excessive gastric immunopathology
physiological function
-
the enzyme is responsible for apoptosis execution in insect cells destined to undergo apoptosis
physiological function
caspase-1 is responsible for the pathogenesis of I/R-induced lung injury as a consequence of mediating endothelial pyroptosis and causing barrier dysfunction
physiological function
caspase-1 is involved in extracellular ATP-mediated immune signaling in fish. It promotes ATP-induced apoptosis
physiological function
the recognition and cleavage of gasdermin D by inflammatory caspases-1, 4, 5, and 11 is an essential step in initiating pyroptosis following inflammasome activation
physiological function
pyroptosis is a mechanism of inflammatory cell death mediated by the activation of the prolytic protein gasdermin D caspase-1 and caspase-11 in mouse. Caspase-1 amplifies inflammation by proteolytic activation of cytokine interleukin-1beta
physiological function
caspase-1 mediates pyroptosis via activation of the prolytic protein gasdermin and amplifies inflammation by proteolytic activation of cytokine interleukin-1beta (IL-1beta)
physiological function
the enzyme is responsible for the pathogenesis of ischemia/reperfusion-induced lung injury as a consequence of mediating endothelial pyroptosis and causing barrier dysfunction
physiological function
pyroptosis is a mechanism of inflammatory cell death mediated by the activation of the prolytic protein gasdermin D by caspase-1, caspase-4, and caspase-5 in human. Caspase-1 amplifies inflammation by proteolytic activation of cytokine interleukin-1beta
physiological function
the enzyme promotes ATP-induced apoptosis. The interactions of inflammatory enzyme with ASC proteins (apoptosis-associated speck-like protein containing a CARD domain) are associated with extracellular ATP-mediated immune signaling
additional information
-
a rapid, high-throughput, single cell, fluorescence-based image analysis method is described utilizing the Amnis ImageStreamX instrument that quantitatively and qualitatively characterizes the frequency, area, and cellular distribution of ASC specks and caspase-1 activity in mouse and human cells. This method differentiates between singular perinuclear specks and false positives. The capacity of our approach to simultaneously detect and quantify ASC specks and caspase-1 activity, both at the population and single-cell level, renders it the most powerful tool available for visualizing and quantifying the impact of mutations on inflammasome assembly and activity
additional information
a rapid, high-throughput, single cell, fluorescence-based image analysis method is described utilizing the Amnis ImageStreamX instrument that quantitatively and qualitatively characterizes the frequency, area, and cellular distribution of ASC specks and caspase-1 activity in mouse and human cells. This method differentiates between singular perinuclear specks and false positives. The capacity of our approach to simultaneously detect and quantify ASC specks and caspase-1 activity, both at the population and single-cell level, renders it the most powerful tool available for visualizing and quantifying the impact of mutations on inflammasome assembly and activity
additional information
-
evaluation is an automated, high-throughput, highly precise computational and quantitative single-cell imaging flow cytometry-based approach that enumerates ASCspeck-containing cells, evaluates specksize,and the localization of caspase-1 activity
additional information
a rapid, high-throughput, single cell, fluorescence-based image analysis method is described utilizing the Amnis ImageStreamX instrument that quantitatively and qualitatively characterizes the frequency, area, and cellular distribution of ASC specks and caspase-1 activity in mouse and human cells. This method differentiates between singular perinuclear specks and false positives. The capacity of our approach to simultaneously detect and quantify ASC specks and caspase-1 activity, both at the population and single-cell level, renders it the most powerful tool available for visualizing and quantifying the impact of mutations on inflammasome assembly and activity
Show AA Sequence and Transmembrane Helices (315 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19000
x * 35000, about, pro-enzyme, SDS-PAGE, x * 23000, about, processed enzyme form 1, SDS-PAGE, x * 19000, about, processed enzyme form 2, SDS-PAGE
23000
x * 35000, about, pro-enzyme, SDS-PAGE, x * 23000, about, processed enzyme form 1, SDS-PAGE, x * 19000, about, processed enzyme form 2, SDS-PAGE
35000
x * 35000, about, pro-enzyme, SDS-PAGE, x * 23000, about, processed enzyme form 1, SDS-PAGE, x * 19000, about, processed enzyme form 2, SDS-PAGE
45000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
monomer or dimer
mature caspase-1 exists predominantly as a monomer under physiological concentration that undergoes dimerization in the presence of substrate
additional information
-
structure of the on-state and the off-state of caspase-1, four of the network H-bonding side chains, Ser332, Ser333, Ser339, and Thr388, form a cluster that lies behind loop 2, consisting of residues 285-290, which contains the catalytic Cys285
?
x * 35000, about, pro-enzyme, SDS-PAGE, x * 23000, about, processed enzyme form 1, SDS-PAGE, x * 19000, about, processed enzyme form 2, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
inactive 45000 Da proform of caspase-1 is basally expressed in macrophages, virus infection induces the cleavage of procaspase into the mature 20000 Da form
proteolytic modification
-
CASP-1 is synthesized as an inactive zymogen and active caspase-1 is produced by proteolytic cleavage of its pro domain, which contains the CAspase Recruitment Domain, i.e. CARD, the CARD domain is localized at the amino end of CASP-1 and serves as a protein-protein interaction module that is important in protein recruitment and proteolytic activation, association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
proteolytic modification
-
pro-caspase-1 is a 45 kDa molecule that autocatalyzes to form active caspase-1, it is also activated by caspase-5
proteolytic modification
-
the inflammasome, a multiprotein complex, regulates caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC
proteolytic modification
-
CASP-1 is synthesized as an inactive zymogen and active caspase-1 is produced by proteolytic cleavage of its pro domain, which contains the CAspase Recruitment Domain, i.e. CARD, the CARD domain is localized at the amino end of CASP-1 and serves as a protein-protein interaction module that is important in protein recruitment and proteolytic activation, association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
proteolytic modification
-
caspase-1 is synthesized as an inactive zymogen that becomes activated by cleavage at aspartic residues to generate an enzymatically active 10-20 kDa heterodimer
proteolytic modification
-
pro-caspase-1 is a 45 kDa molecule that autocatalyzes to form active caspase-1, it is also activated by caspase-11
proteolytic modification
-
the inflammasome, a multiprotein complex, regulates caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC
proteolytic modification
-
CASP-1 is synthesized as an inactive zymogen and active caspase-1 is produced by proteolytic cleavage of its pro domain, which contains the CAspase Recruitment Domain, i.e. CARD, the CARD domain is localized at the amino end of CASP-1 and serves as a protein-protein interaction module that is important in protein recruitment and proteolytic activation, association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
proteolytic modification
-
pro-caspase-1 is a 45 kDa molecule that autocatalyzes to form active caspase-1
proteolytic modification
the proenzyme of Sf caspase-1 is 299 amino acids in length and can undergo autocatalytic processing in Escherichia coli to an active enzyme heterocomplex. Autoprocessing occurs at Asp28-, Asp184, and Asp95 to generate the large p19/p18 and the small p12 subunits
proteolytic modification
-
pro-Sf-caspase-1 with a short domain is activated by an apical caspase through proteolytic cleavage, at the caspase-recognition site between the large and small subunits of pro-Sfcaspase-1, when apoptotic signaling is triggered
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
active forms of caspase-1 bound to the active-site inhibitors Ac-WEHD-CHO and z-Val-Ala-Asp-fluoromethylketone, or active-site ligand-free enzyme, the active-site ligand-free and allosterically inhibited conformations are nearly identical, hanging-drop vapor diffusion at 4°C against a reservoir containing for mutant R286K: 0.1 M 1,4-piperazinediethanesulfonic acid, pH 6.0, 200 mM Li2SO4, 25% PEG 2000 MME, 10 mM DTT, 3 mM NaN3, and 2 mM MgCl2, or for mutant E390D: 0.1 M Pipes, pH 6.0, 350 mM (NH4)2SO4, 20% PEG 2000 MME, 10 mM DTT, 3 mM NaN3, and 2 mM MgCl2, or for mutant R286K/E390D: 0.1 M Pipes, pH 6.0, 175 mM (NH4)2SO4, 20% PEG 2000 MME, 10 mM DTT, 3 mM NaN3, and 2 mM MgCl, X-ray diffraction structure determination and analysis at 1.8-2.1 A resolution, molecular replacement
-
enzyme mutants in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid, hanging drop vapor diffusion method, using 0.1 M PIPES pH 6.0, 75-175 mM (NH4)2SO4, 25% (w/v) PEG 2000 MME, 10 mM dithiothreitol, 3 mM NaN3, and 2 mM MgCl2
mutant enzyme C285A in complex with full-length murine gasdermin D, hanging drop vapor diffusion method, using 20% (w/v) PEG3350, 0.2 M ammonium citrate tribasic, pH 7.0, and 5 mM dithiothreitol
sitting drop vapor diffusion method at 4°C, crystal structure of a complex between human caspase-1 and the full-length murine gasdermin D
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A329T
C136S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C169S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C244S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C270S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C285A
C285S
C331S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C362S
-
the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C362S/C397S
-
the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C364S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C397S
-
the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C69S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C72S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C77S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
D297A
-
site-directed mutagenesis, mutation at the D297 residue abolishes the effect of caspase-1 on RIG-I
D316A
-
site-directed mutagenesis, mutation at the D316 residue does not abolish the effect of caspase-1 on RIG-I
D336A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
E390A
-
site-directed mutagenesis, the mutant shows an about 130fold loss of catalytic efficiency compared to the wild-type enzyme
K319R
L265S
N263S
N337A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
R221C
R240Q
R286A
-
site-directed mutagenesis, the mutant shows an about 230fold loss of catalytic efficiency compared to the wild-type enzyme
R286K
-
site-directed mutagenesis, the mutant shows an about 150fold loss of catalytic efficiency compared to the wild-type enzyme
R286K/E390D
-
site-directed mutagenesis, the mutant shows an about 37fold loss of catalytic efficiency compared to the wild-type enzyme
S332A
-
site-directed mutagenesis, the mutant shows an about 4fold loss of catalytic efficiency compared to the wild-type enzyme
S333A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
S339A
-
site-directed mutagenesis, the mutant shows an about 7fold loss of catalytic efficiency compared to the wild-type enzyme
T267I
T334A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
T388A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
additional information
A329T
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
C285A
-
a procaspase-1 variant with decreased enzymatic activity showing about 3.5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
C285S
-
site-directed mutagenesis, in comparison to wild type procaspase-1, expression of the C285S mutant does not alter the cellular levels of the RIG-I protein
C285S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
K319R
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
K319R
-
a procaspase-1 variant with decreased enzymatic activity showing about 1.6fold increased nuclear factor-kappaB activation compared to the wild type enzyme
L265S
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
L265S
-
a procaspase-1 variant with decreased enzymatic activity showing about 6.5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
N263S
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
N263S
-
a procaspase-1 variant with decreased enzymatic activity showing about 1.8fold increased nuclear factor-kappaB activation compared to the wild type enzyme
R221C
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
R240Q
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
R240Q
-
a procaspase-1 variant with decreased enzymatic activity showing about 5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
T267I
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
additional information
-
genetic disruption of cryopyrin or the adaptor apoptosis associated speck-like protein, ASC, abrogates caspase-1 activation in poly(I:C), dsRNA, or viral RNA-stimulated macrophages
additional information
-
secretion of interleukin-1beta following KIM5 infection is reduced in caspase-1-deficient macrophages compared to wild-type macrophages
additional information
-
caspase-1-/- bone marrow-derived macrophages exhibit strong caspase-3 expression and reduced cell damage compared to wild-type cells during early Burkholderia pseudomallei infection, indicating classical apoptosis, whereas wild-type bone marrow-derived macrophages show signs of rapid caspase-1-dependent cell death. Caspase-1-/- bone marrow-derived macrophages exhibit impaired bactericidal activity compared to wild-type bone marrow-derived macrophages
additional information
-
caspase-1-deficient macrophages show only slightly reduced ATP-triggered MHC-II secretion, overview
additional information
-
Salmonella- and lipopolysaccharide-, and ATP-induced activation of caspase-7 is abolished in macrophages deficient in caspase-1, the pattern recognition receptors Ipaf and Cryopyrin, and the inflammasome adaptor ASC
additional information
-
caspase-1-deficient mice have unimpaired inflammatory responses to necrotic cells
additional information
-
defective Anthrax-induced interleukin-1beta secretion in Nod2-/- or caspase-1-/- macrophages, not due to decreased pro-interleukin-1beta expression, caspase-1 or NOD2 deficiencies do not exert a major effect on TNF-alpha secretion
additional information
-
caspase-1-deficient macrophages show only slightly reduced ATP-triggered MHC-II secretion, overview
-
additional information
-
Salmonella- and lipopolysaccharide-, and ATP-induced activation of caspase-7 is abolished in macrophages deficient in caspase-1, the pattern recognition receptors Ipaf and Cryopyrin, and the inflammasome adaptor ASC
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant caspase-1 solubilized from insoluble inclusion bodies from Escherichi coli by cation exchange chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and sequencing of ICE-related cDNAs encoding hybrid caspase-1/caspase-13-like propeptides
co-expression of caspase-1 with wild-type and mutant, myc-tagged B30.2 domain-deleted pyrin, in PT67 cells, co-expression of wild-type pyrin, caspase-1, and interleukin-1beta in COS-7 cells
-
DNA and amino acid sequence determination and analysis, sequence comparison, expression of the His-tagged Tn-caspase-1 in Trichoplusia ni using the baculovirus transfection system
DNA sequence analysis
dog inflammatory caspase, DNA and amino acid sequence determination and analysis, the nucleotide sequence encoding the ORF of the dog inflammatory caspase, corresponding to SwissProt ID Q9MZV7 limits 132 to 404, is codon optimized, the dog genome contains a single caspase-1 and caspase-4-like gene. The gene encodes a protein called hybrid caspase-1/caspase-4 or hybrid inflammatory caspase, which contains a caspase-1 CARD followed by a caspase-4 CARD and catalytic domain, recombinant expression in Escherichia coli strain BL21(DE3)
expressed in baculovirus infected insect cells as 30000 Da proteins lacking the propeptide, automaturation into p20 and p10 subunits
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Star cells as insoluble inclusion bodies
expression in Escherichia coli
expression of GST-tagged procaspase-1, -3 and -4 cDNAs in Hep-G2 cells, overexpression of caspase-1 decreases cellular levels of RIG-I protein, while the overexpression of procaspase-3 does not have effects on RIG-I protein expression, overview
-
transient co-expression of of FALG-tagged NOD2, Myc-tagged caspase-1, and pro-interleukin-1beta in HEK293T cells allows muramyl dipeptide-induced pro-interleukin-1beta processing
-
transient coexpression of caspase wild-type parkin in HEK-293 cells identifies caspase-1, caspase-3 and caspase-8 as efficient inducers of parkin cleavage
-
transient transfection of HEK-293 cells with the caspase-1-V5/His fusion protein
-
cloning and sequencing of ICE-related cDNAs encoding hybrid caspase-1/caspase-13-like propeptides
cloning and sequencing of ICE-related cDNAs encoding hybrid caspase-1/caspase-13-like propeptides
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an approximately 32fold increase in caspase-1 expression is observed in the p53-knockin cell line H273
caspase-1 is upregulated in CD8+ cells with decreased expression of interleukin-4 and interleukin-10
-
macrophages from A/J mice exhibit reduced caspase-1 activation and IL-1beta secretion compared to C57BL/6 macrophages
-
the activation of caspase-1 is markedly inhibited with increasing concentrations of extracellular KCl
-
the expression of EcASC and EcCaspase-1 was significantly upregulated in response to ATP infection
the region of difference 1 locus in the Mycobacterium tuberculosis genome contributes to activation of caspase-1 via induction of potassium ion efflux in infected macrophages
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the transcript of caspase-1 and its protein products appear in two or more waves in the midgut during metamorphosis
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
50 mM HEPES (pH 8.0), 100 mM NaCl, 10% (w/v) sucrose, 1 M nondetergent sulfobetaine 201, and 10 mM dithiothreitol
recombinant caspase-1 from Escherichi coli expressed in insoluble inclusion bodies
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
ICE activity is a possible target for fighting excessive inflammatory conditions
medicine
-
the caspase-1/IL-1beta signaling pathway plays an important role in diabetes-induced retinal pathology, and its inhibition might represent a new strategy to inhibit capillary degeneration in diabetic retinopathy
EXTERNAL LINKS (specific for EC-Number 3.4.22.36)
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Release 2026.1 (March 2026)
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