Information on EC 3.4.22.36 - caspase-1

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The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY
3.4.22.36
-
RECOMMENDED NAME
GeneOntology No.
caspase-1
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-/-
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C14.001
-
-
-
-
CASP-1
-
-
-
-
ICE
-
-
-
-
IL-1 beta converting enzyme
-
-
-
-
IL-1BC
-
-
-
-
interleukin-1 beta converting enzyme
-
-
-
-
interleukin-1beta-converting enzyme
-
-
-
-
p45
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
122191-40-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
adult, male C57BL/6 mice
-
-
Manually annotated by BRENDA team
Balb/c mice
-
-
Manually annotated by BRENDA team
BALB/cJ mice
-
-
Manually annotated by BRENDA team
C57BL/6 and BALB/c mice
-
-
Manually annotated by BRENDA team
female C57BL/6 mice
-
-
Manually annotated by BRENDA team
mutant mouse bearing amino acid differences in Naip5, one of the NOD-like receptors (NLRs), one of the adaptor proteins for caspase-1 activation
-
-
Manually annotated by BRENDA team
strain C3H/An
SwissProt
Manually annotated by BRENDA team
Mus musculus BALB/c
Balb/c mice
-
-
Manually annotated by BRENDA team
Mus musculus BALB/cJ
BALB/cJ mice
-
-
Manually annotated by BRENDA team
Mus musculus C3H/An
strain C3H/An
SwissProt
Manually annotated by BRENDA team
Mus musculus C57BL/6
C57BL/6 mice
-
-
Manually annotated by BRENDA team
Sprague Dawley
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
-
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
physiological function
-
caspase 1 is a major regulator of the inflammation response
physiological function
-
caspase-1 is dispensable for interleukin-33 release by macrophages
physiological function
-
caspase-1 is mainly involved in cytokine maturation, leading to an inflammatory response
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
-
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
-
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
-
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
-
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
-
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(Z-LEHD)2-R110 tetrapeptide + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
P29466
-
-
-
?
Ac-LEHD-7-amido-4-methylcoumarin + H2O
Ac-LEHD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Ac-Trp-Glu-His-Asp-7-amino-4-trifluoromethylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Ac-YVAD-4-nitroanilide + H2O
Ac-YVAD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-DEVD-4-nitroanilide + H2O
acetyl-DEVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-DQMD-4-nitroanilide + H2O
acetyl-DQMD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
acetyl-VEID-4-nitroanilide + H2O
acetyl-VEID + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-VQVD-4-nitroanilide + H2O
acetyl-VQVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-WEHD-7-amido-4-methylcoumarin + H2O
acetyl-WEHD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
-
acetyl-WEHD-7-amido-4-methylcoumarin + H2O
acetyl-WEHD + 7-amino-4-methylcoumarin
show the reaction diagram
-
WEHD is the optimal tetrapeptide recognition motif
-
-
?
acetyl-YEVD-4-nitroanilide + H2O
acetyl-YEVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-YEVDGW-amide + H2O
?
show the reaction diagram
-
preferred peptide substrate
-
-
?
acetyl-YVAD-4-nitroanilide + H2O
acetyl-YVAD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
show the reaction diagram
P29466
-
-
-
?
Assc2 peptide + H2O
?
show the reaction diagram
-
-
-
-
?
ataxin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
Bcl-xL + H2O
?
show the reaction diagram
-
-
-
-
?
beta-actin + H2O
?
show the reaction diagram
-
-
-
-
?
beta-actin + H2O
?
show the reaction diagram
-
-
-
-
?
beta-actin + H2O
?
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
calpastatin + H2O
?
show the reaction diagram
-
-
-
-
?
caspase-1 + H2O
?
show the reaction diagram
-
-
-
-
?
cPLA2 peptide + H2O
?
show the reaction diagram
-
-
-
-
?
cyclin G-associated kinase + H2O
?
show the reaction diagram
-
-
-
-
?
DNA replication licensing factor MCM4 + H2O
?
show the reaction diagram
-
-
-
-
?
elF-4H peptide + H2O
?
show the reaction diagram
-
-
-
-
?
endoplasmin + H2O
?
show the reaction diagram
-
-
-
-
?
epidermal growth factor receptor + H2O
?
show the reaction diagram
-
cleavage during apoptosis
-
-
?
eukaryotic translation initiation factor 3 subunit J + H2O
?
show the reaction diagram
-
-
-
-
?
FLP-1 peptide + H2O
?
show the reaction diagram
-
-
-
-
?
FYN-binding protein + H2O
?
show the reaction diagram
-
-
-
-
?
GADPH + H2O
?
show the reaction diagram
-
-
-
-
?
gamma-actin + H2O
?
show the reaction diagram
-
-
-
-
?
gasdermin D + H2O
?
show the reaction diagram
-
-
-
-
?
GIT2 peptide + H2O
?
show the reaction diagram
-
-
-
-
?
heat shock protein 60 + H2O
?
show the reaction diagram
-
-
-
-
?
histone E3 peptide + H2O
?
show the reaction diagram
-
-
-
-
?
HnRNP + H2O
?
show the reaction diagram
-
-
-
-
?
Hsp90 + H2O
?
show the reaction diagram
-
-
-
-
?
IL-1 beta + H2O
?
show the reaction diagram
-
-
-
-
?
IL-18 + H2O
?
show the reaction diagram
-
-
-
-
?
IL1F7 + H2O
?
show the reaction diagram
-
-
-
-
?
interferon-gamma inducing factor + H2O
?
show the reaction diagram
-
cleavage site: LESD-/-
-
-
?
interleukin-1 + H2O
interleukin-1beta
show the reaction diagram
-
-
-
-
?
interleukin-18 + H2O
?
show the reaction diagram
-
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
-
-
?
interleukin-1beta + H2O
?
show the reaction diagram
-
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
-
-
?
ligatin + H2O
?
show the reaction diagram
-
-
-
-
?
LMNA Isoform + H2O
?
show the reaction diagram
-
-
-
-
?
MAP-tau Isoform + H2O
?
show the reaction diagram
-
-
-
-
?
MyD88 adaptor-like + H2O
?
show the reaction diagram
-
NF-kappaB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1
-
-
?
MyD88 adaptor-like + H2O
?
show the reaction diagram
-
caspase-1 cleaves the TLR adaptor MyD88 adaptor-like at position D198
-
-
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
B6EEC1
-
-
-
?
Nedd4 + H2O
?
show the reaction diagram
-
-
-
-
?
nuclear immunophilin FKBP46 + H2O
?
show the reaction diagram
P89116
-
-
-
?
p35 + H2O
100000 Da fragment + 25000 Da fragment
show the reaction diagram
P89116
cleavage at Asp87
-
?
parkin + H2O
?
show the reaction diagram
-
-
-
-
?
parkin + H2O
?
show the reaction diagram
-
cleavage at Asp126-Ser127, 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
-
-
?
PARP + H2O
?
show the reaction diagram
-
-
-
-
?
periphilin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
PLA2G4A + H2O
?
show the reaction diagram
-
-
-
-
?
poly(ADP-ribose)polymerase + H2O
?
show the reaction diagram
P29466
-
-
-
?
PPARgamma + H2O
?
show the reaction diagram
-
-
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
virus infection by influenza A or Sendai virus induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
-
-
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
-
-
-
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
-
-
-
-
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
P29452
-
-
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
P29466
cleavage to the mature interleukin-1beta
-
-
-
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
Mus musculus C3H/An
P29452
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
PREL-1 peptide + H2O
?
show the reaction diagram
-
-
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
show the reaction diagram
-
activation
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
caspase-1-mediates activation of endogenous caspase-7
-
-
?
pro-caspase-7 + H2O
caspase-7 + amino-terminal procaspase-7 peptide
show the reaction diagram
-
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
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
activation
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
activation of caspase-1 as a key event resulting in interleukin-18 production, caspase-1 is essential for interleukin-18 production in infected macrophages
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
active caspase-1 converts inactive pro-interleukin-18 to active interleukin-18
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
Mus musculus BALB/c
-
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
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
P29452
pIL-1beta is mainly processed by caspase-1, but also by caspase-3
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
-
caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
-
pro-interleukin-1beta cleavage site 1 is FEAD-/-, pro-interleukin-1beta cleavage site II is YVHD-/-
-
-
-
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
Mus musculus C3H/An
P29452
pIL-1beta is mainly processed by caspase-1, but also by caspase-3
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
activation
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
caspase-1 activation leads to release of active interleukin-1beta from THP-1 cells, regulation, overview
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
caspase-1 is the enzyme responsible for the cleavage and activation of interleukin-1beta, which is a potent pro-inflammatory cytokine
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
active caspase-1 converts inactive 31 kDa pro-interleukin-1beta to 18 kDa active interleukin-1beta
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
cleavage between Asp116 and Ala117, required for activation of the cytokine
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
Mus musculus BALB/c
-
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
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
caspase-1 effectively cleaves interleukin-1beta to its mature form in both heat shock and 37C conditions
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
Mus musculus BALB/cJ
-
caspase-1 effectively cleaves interleukin-1beta to its mature form in both heat shock and 37C conditions
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
Mus musculus C57/Bl
-
-
-
-
?
pro-interleukin-33 + H2O
interleukin-33 + ?
show the reaction diagram
-
activation
-
-
?
pro-interleukin-33 + H2O
mature interleukin-33 + ?
show the reaction diagram
-
recombinant pro-interleukin-33 is cleaved by recombinant caspase-1 in vitro
-
-
?
PSEN1 + H2O
?
show the reaction diagram
-
-
-
-
?
PSEN2 + H2O
?
show the reaction diagram
-
-
-
-
?
pyrin + H2O
?
show the reaction diagram
-
-
-
-
?
pyrin + H2O
?
show the reaction diagram
-
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, recombinant substrate expressed in PT67 cells
-
-
?
SMG7 peptide + H2O
?
show the reaction diagram
-
-
-
-
?
sphingosine kinase 2 + H2O
?
show the reaction diagram
-
-
-
-
?
splicing factor U2AF 65-kDa subunit + H2O
?
show the reaction diagram
-
-
-
-
?
SPTAN1 + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-YVAD-4-nitroanilide + H2O
succinyl-YVAD + 4-nitroaniline
show the reaction diagram
P29466
-
-
-
?
succinyl-YVAD-4-nitroanilide + H2O
succinyl-YVAD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-YVAD-7-amido-4-methylcoumarin + H2O
succinyl-YVAD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
synapse-associated protein 1 + H2O
?
show the reaction diagram
-
-
-
-
?
target of Myb protein 1 pepitde + H2O
?
show the reaction diagram
-
-
-
-
?
TF AP-2alpha + H2O
?
show the reaction diagram
-
-
-
-
?
TIF1b peptide + H2O
?
show the reaction diagram
-
-
-
-
?
Trp-Glu-His-Asp-p-nitroanilide + H2O
Trp-Glu-His-Asp + p-nitroaniline
show the reaction diagram
-
-
-
-
?
Vsp72 peptide + H2O
?
show the reaction diagram
-
-
-
-
?
WEDH + H2O
?
show the reaction diagram
-
-
-
-
?
zyxin + H2O
?
show the reaction diagram
-
-
-
-
?
MCM3 peptide + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme is involved in cytokine activation
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the production of the active enzyme induces the activation of an endogenous 32000 Da (CPP32) like caspase
-
-
-
additional information
?
-
O02002
cell death protease essential for development. Loss of zygotic caspase-1 function in Drosophila causes larval lethality and melanotic tumors
-
-
-
additional information
?
-
P89116
the enzyme is able to induce apoptosis in Sf9 cells
-
-
-
additional information
?
-
P29452
the enzyme induces apoptosis in transfected cells
-
-
-
additional information
?
-
-
caspase 1 activated by protease-activating factor acts upstream of mitochondria to cause release of proteins that are known to mediate apoptosis
-
-
-
additional information
?
-
-
caspase-1 is an upstream positive regulator of caspase-6-mediated cell death in primary human neurons
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
-
-
-
additional information
?
-
-
caspase-1 is a negative regulator of AMPA receptor-mediated long-term potentiation at hippocampal synapses
-
-
-
additional information
?
-
-
caspase-1 is critical for IFN-gamma-mediated control of Anaplasma phagocytophilum infection
-
-
-
additional information
?
-
-
caspase-1 is important in the host response to sepsis at least in part via its ability to regulate sepsis-induced splenic cell apoptosis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
-
-
-
additional information
?
-
-
functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1 activation contributes to the development of nitrogen-containing bisphosphonate-associated inflammatory side effects including jaw osteomyelitis, overview
-
-
-
additional information
?
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
-
-
-
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 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1 is involved in this apoptosis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
-
-
-
additional information
?
-
-
critical involvement of pneumolysin in production of interleukin-1alpha and caspase-1-dependent cytokines in infection with Streptococcus pneumoniae in vitro
-
-
-
additional information
?
-
-
enzyme regulation, mechanisms of ATP-induced and caspase-1-dependent cell death and interleukin-1beta release are both regulated by zinc, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
mevalonate kinase deficiency patients have overactive caspase-1, causing enhanced interleukin-1beta processing and subsequent inflammation in response to bacterial components
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
pro-inflammatory cytokine interleukin-18 and its activator caspase-1 are involved in acute liver failure and acute-on-chronicliver-failure
-
-
-
additional information
?
-
-
pyrin and caspase-1 interact in their pathway for NF-kappaB activation, mechanism and regulation, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
peptide substrate screening, the enzyme preferably cleaves after Asp, overview
-
-
-
additional information
?
-
-
caspase-1-cleaved peptides show propensity for hydrophobic residues at P4
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Mus musculus C3H/An
P29452
the enzyme induces apoptosis in transfected cells
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
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
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
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
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
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, peptide substrate screening, the enzyme preferably cleaves after Asp, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
epidermal growth factor receptor + H2O
?
show the reaction diagram
-
cleavage during apoptosis
-
-
?
interferon-gamma inducing factor + H2O
?
show the reaction diagram
-
cleavage site: LESD-/-
-
-
?
interleukin-1 + H2O
interleukin-1beta
show the reaction diagram
-
-
-
-
?
interleukin-18 + H2O
?
show the reaction diagram
-
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
-
-
?
MyD88 adaptor-like + H2O
?
show the reaction diagram
-
NF-kappaB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1
-
-
?
MyD88 adaptor-like + H2O
?
show the reaction diagram
-
caspase-1 cleaves the TLR adaptor MyD88 adaptor-like at position D198
-
-
?
nuclear immunophilin FKBP46 + H2O
?
show the reaction diagram
P89116
-
-
-
?
p35 + H2O
100000 Da fragment + 25000 Da fragment
show the reaction diagram
P89116
cleavage at Asp87
-
?
parkin + H2O
?
show the reaction diagram
-
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
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
virus infection by influenza A or Sendai virus induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
show the reaction diagram
-
activation
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
show the reaction diagram
Mus musculus, Mus musculus C57BL/6
-
caspase-1-mediates activation of endogenous caspase-7
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
activation
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
activation of caspase-1 as a key event resulting in interleukin-18 production, caspase-1 is essential for interleukin-18 production in infected macrophages
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
Mus musculus BALB/c
-
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
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
P29452
pIL-1beta is mainly processed by caspase-1, but also by caspase-3
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
-
caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
-
pro-interleukin-1beta cleavage site 1 is FEAD-/-, pro-interleukin-1beta cleavage site II is YVHD-/-
-
-
-
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
activation
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
caspase-1 activation leads to release of active interleukin-1beta from THP-1 cells, regulation, overview
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
caspase-1 is the enzyme responsible for the cleavage and activation of interleukin-1beta, which is a potent pro-inflammatory cytokine
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
-
caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
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
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
Mus musculus C3H/An
P29452
pIL-1beta is mainly processed by caspase-1, but also by caspase-3
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
Mus musculus BALB/c
-
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
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
Mus musculus C57BL/6
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
Mus musculus BALB/cJ
-
-
-
-
?
pro-interleukin-33 + H2O
interleukin-33 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-33 + H2O
mature interleukin-33 + ?
show the reaction diagram
-
recombinant pro-interleukin-33 is cleaved by recombinant caspase-1 in vitro
-
-
?
pyrin + H2O
?
show the reaction diagram
-
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
-
-
?
sphingosine kinase 2 + H2O
?
show the reaction diagram
-
-
-
-
?
interleukin-1beta + H2O
?
show the reaction diagram
-
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
-
-
?
additional information
?
-
-
the enzyme is involved in cytokine activation
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the production of the active enzyme induces the activation of an endogenous 32000 Da (CPP32) like caspase
-
-
-
additional information
?
-
O02002
cell death protease essential for development. Loss of zygotic caspase-1 function in Drosophila causes larval lethality and melanotic tumors
-
-
-
additional information
?
-
P89116
the enzyme is able to induce apoptosis in Sf9 cells
-
-
-
additional information
?
-
P29452
the enzyme induces apoptosis in transfected cells
-
-
-
additional information
?
-
-
caspase 1 activated by protease-activating factor acts upstream of mitochondria to cause release of proteins that are known to mediate apoptosis
-
-
-
additional information
?
-
-
caspase-1 is an upstream positive regulator of caspase-6-mediated cell death in primary human neurons
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
-
-
-
additional information
?
-
-
caspase-1 is a negative regulator of AMPA receptor-mediated long-term potentiation at hippocampal synapses
-
-
-
additional information
?
-
-
caspase-1 is critical for IFN-gamma-mediated control of Anaplasma phagocytophilum infection
-
-
-
additional information
?
-
-
caspase-1 is important in the host response to sepsis at least in part via its ability to regulate sepsis-induced splenic cell apoptosis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
-
-
-
additional information
?
-
-
functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1 activation contributes to the development of nitrogen-containing bisphosphonate-associated inflammatory side effects including jaw osteomyelitis, overview
-
-
-
additional information
?
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
-
-
-
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 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1 is involved in this apoptosis
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
-
-
-
additional information
?
-
-
critical involvement of pneumolysin in production of interleukin-1alpha and caspase-1-dependent cytokines in infection with Streptococcus pneumoniae in vitro
-
-
-
additional information
?
-
-
enzyme regulation, mechanisms of ATP-induced and caspase-1-dependent cell death and interleukin-1beta release are both regulated by zinc, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
mevalonate kinase deficiency patients have overactive caspase-1, causing enhanced interleukin-1beta processing and subsequent inflammation in response to bacterial components
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
pro-inflammatory cytokine interleukin-18 and its activator caspase-1 are involved in acute liver failure and acute-on-chronicliver-failure
-
-
-
additional information
?
-
-
pyrin and caspase-1 interact in their pathway for NF-kappaB activation, mechanism and regulation, overview
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-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
caspase-1-cleaved peptides show propensity for hydrophobic residues at P4
-
-
-
additional information
?
-
Mus musculus C3H/An
P29452
the enzyme induces apoptosis in transfected cells
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
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
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
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
-
-
-
additional information
?
-
Mus musculus C57BL/6
-
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
-
-
-
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
INHIBITORS
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)-2-(4'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-((S)-2-((S)-2-(2-naphthamido)-3-methylbutanamido)-propanamido)-4-(2-hydroxy)benzylaminobutanoic acid
-
-
(S)-3-(2'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-(2-naphthalen-1-yl-benzenesulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-(3'-acetylamino-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-(3'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-(6-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-(biphenyl-2-sulfonylamino)-4-oxobutyric acid
-
-
(S)-3-benzenesulfonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
(S)-3-benzenesulfonylamino-4-oxo-9-phenyl-nonanoic acid
-
-
(S)-3-benzyloxycarbonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
(S)-3-benzyloxycarbonylamino-4-oxo-9-phenyl-nonanoic acid
-
-
(S)-3-benzynesulfonylamino-4-oxo-butyric 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)-4-oxo-9-phenylnonanoic 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-WEHD-CHO
-
active-site inhibitor
Ac-YVAD-chloromethyl ketone
-
-
Ac-YVAD-chloromethylketone
-
inhibition of caspase-1 with Ac-YVAD-CMK prevents SphK2 cleavage
Ac-YVAD-CHO
-
a caspase-1 inhibitor
acetyl-AEVD-aldehyde
-
-
acetyl-Ala-Pro-Nle-Asp-aldehyde
-
-
acetyl-DEVD-aldehyde
-
-
acetyl-DEVS-aldehyde
-
-
acetyl-IETD-aldehyde
-
-
acetyl-L-Leu-L-Glu-L-His-L-Asp-CHO
-
-
acetyl-L-Tyr-L-Val-L-Ala-L-Asp
-
-
acetyl-L-Tyr-L-Val-L-Ala-L-Asp-2,6-dimethylbenzoyloxymethylketone
-
-
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
acetyl-Tyr-Val-Ala-Asp-chloromethylketone
-
-
acetyl-Tyr-Val-Ala-Asp-chloromethylketone
-
-
acetyl-Tyr-Val-Ala-Asp-CHO
-
-
acetyl-Tyr-Val-Ala-Asp-CO-(CH2)5-Ph
-
-
acetyl-WEHD-aldehyde
-
-
acetyl-YVAD-aldehyde
-
-
acetyl-YVAD-aldehyde
-
-
acetyl-YVAD-chloromethylketone
-
-
acetyl-YVAD-CHO
-
caspase-1 specific inhibitor
benzyloxycarbonyl-Pro-Nle-Asp-aldehyde
-
-
-
benzyloxycarbonyl-VAD-CHO
-
-
benzyloxycarbonyl-VAD-fluoromethylketone
-
t1/2 at 0.001 mM is 2.5 s
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
-
-
benzyloxycarbonyl-YVAD-fluoromethylketone
-
-
butyloxycarbonyl-Asp-chloromethylketone
-
-
butyloxycarbonyl-Asp-fluoromethylketone
-
-
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
carbobenzoxy-valylalanyl-aspartyl-fluoromethylketone
-
-
carbobenzyloxy-Asp-Glu-Val-Asp-fluoromethyl ketone
-
specific to suppress the activity of Sf-caspase-1 by blocking amplification of Sfcaspase-1
carbobenzyloxy-Trp-Glu-His-Asp-fluoromethylketone
-
-
carbobenzyloxy-VAD-fluoromethyl ketone
-
pan-caspase inhibitor
carbobenzyloxy-VAD-fluoromethyl ketone
-
pan-caspase inhibitor
carbobenzyloxy-Val-Ala-Asp-fluoromethyl ketone
-
a broad-spectrum inhibitor of initiator caspase
carbobenzyloxy-WEHD-fluoromethyl ketone
-
caspase-1-specific inhibitor
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
-
cowpox serpin CrmA
-
-
-
DEVD-fluoromethylketone
-
-
Disulfiram
-
inhibits the enzyme
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
Glu-Val-Asp-aldehyde
-
-
IDN-6556
-
active-site inhibitor that acts through irreversible covalent modification of the catalytic cysteine residue
IDN-6556
-
-
iodoacetamide
-
-
kaempferol
-
-
L-Tyr-L-Val-L-Ala-L-Asp-chloromethylketone
-
-
L-Tyr-L-Val-L-Ala-L-Asp-CHO
-
caspase-1-specific inhibitor
L-Tyr-L-Val-L-Ala-L-Asp-CN
-
-
luteolin
-
-
myricetin
-
-
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-benzyloxycarbonyl-Tyr-Val-Ala-Asp-fluoromethyl ketone
-
-
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
p35
P89116
IC50: 0.5 nM
-
pralnacasan
-
a specific caspase-1 inhibitor
pralnacasan
-
potent caspase 1 inhibitor
pralnacasan
-
VX-740, active-site inhibitor that acts through reversible covalent modification of the catalytic cysteine residue
pralnacasan
-
-
quercetin
-
-
ritonavir
-
blocks caspase-1 activation and inhibits the enzyme
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
tetracycline
-
-
VRT-043198
-
-
YN-1234
-
i.e. N-2-naphthoyl-L-valyl-N-[(1S)-2-carboxy-1-formylethyl]-L-prolinamide
YVAD-chloromethyl ketone
-
-
YVAD-chloromethylketone
-
-
Z-L-Tyr-L-Val-L-Ala-L-Asp-fluoromethylketone
-
specific inhibitor for caspase-1, complete inhibition at 0.05 mM
Z-L-Val-L-Ala-L-Asp-(O-methyl)-fluoromethylketone
-
-
Z-L-Val-L-Ala-L-Asp-fluoromethylketone
-
broad-spectrum caspase inhibitor
Z-Trp-Glu-His-Asp-fluoromethylketone
-
-
Z-Val-Ala-ASp-fluoromethylketone
-
broad-range caspase inhibitor
Z-WEHD-fluoromethylketone
-
-
Z-YVAD-fluoromethylketone
-
-
minocycline
-
-
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
-
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
-
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
-
hypoxia abrogates caspase-1 inhibition, overview
-
additional information
-
caspase-1 is not inhibited by Asp-Glu-Val-Asp-CHO, Ile-Glu-Thr-Asp-CHO, and Leu-Glu-His-Asp-CHO
-
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
-
chromogranin A
-
chromogranin A can activate pro-caspase-1 in microglia
-
Ipaf
-
i.e. host nucleotide-binding domain and leucine-rich repeatcontaining protein Ipaf or NLRC4, Ipaf-dependent activation is unaffected by potassium treatment
-
lipopolysaccharide
-
-
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
-
NLRC4 inflammasome
-
-
-
NLRP1 inflammasome
-
-
-
NLRP3 inflammasome
-
-
-
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
-
poly(dA-dT)
-
-
-
protease activating factor
-
i.e. Ipaf. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf
-
protease-activating factor
-
activates caspase 1 in p53-dependent apoptosis
-
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
Urate
-
-
monosodium urate
-
-
-
additional information
-
activation of the Rac1/PI3K/protein kinase B pathway is required for caspase-1 activation mediating increased interleukin-1beta release
-
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
-
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
-
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
-
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
-
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
-
activation of caspase-1 in macrophages occurs independently of Nalp3 and proteasome activity
-
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
-
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 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
-
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
-
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
-
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
-
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 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
-
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
-
the inflammasome activator ATP can induce the production of reactive oxygen species, which are important for caspase-1 activation
-
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
-
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
0.045
acetyl-DQMD-4-nitroanilide
-
pH 7.5, 30C
0.0085
acetyl-LEVD-4-nitroanilide
-
pH 7.5, 30C
0.018
acetyl-LEVD-4-nitroanilide
-
pH 7.5, 30C
0.046
acetyl-VEID-4-nitroanilide
-
pH 7.5, 30C
0.12
acetyl-VQVD-4-nitroanilide
-
pH 7.5, 30C
0.004
acetyl-WEHD-7-amido-4-methylcoumarin
-
pH 7.5
0.0073
acetyl-YEVD-4-nitroanilide
-
pH 7.5, 30C
0.105
acetyl-YEVDGW-amide
-
pH 7.5, 30C
0.023
acetyl-YVAD-4-nitroanilide
-
pH 7.5, 30C
0.000004
pro-interleukin-1beta
-
pH 7.5
-
0.0000215
succinyl-YVAD-4-nitroanilide
-
pH 7.5
0.006
succinyl-YVAD-4-nitroanilide
-
pH 7.5, 37C
0.02
succinyl-YVAD-7-amido-4-methylcoumarin
-
pH 7.5, 37C
0.0000115
acetyl-YVAD-7-amido-4-methylcoumarin
-
pH 7.5
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
-
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
13
acetyl-WEHD-7-amido-4-methylcoumarin
-
pH 7.5
1.2
pro-interleukin-1beta
-
pH 7.5
-
1
succinyl-YVAD-4-nitroanilide
-
pH 7.5, 37C
1.6
succinyl-YVAD-4-nitroanilide
-
pH 7.5
0.35
succinyl-YVAD-7-amido-4-methylcoumarin
-
pH 7.5, 37C
1
acetyl-YVAD-7-amido-4-methylcoumarin
-
pH 7.5
additional information
additional information
-
-
-
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
(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
-
-
0.0024
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)hexanoyl]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
-
-
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
-
-
0.0072
(S)-2-(4'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric 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 30C
0.0068
(S)-3-(2'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
0.0069
(S)-3-(2-naphthalen-1-yl-benzenesulfonylamino)-4-oxo-butyric acid
-
-
0.0023
(S)-3-(3'-acetylamino-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
0.0031
(S)-3-(3'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
0.0019
(S)-3-(6-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
0.0016
(S)-3-(biphenyl-2-sulfonylamino)-4-oxobutyric acid
-
-
0.024
(S)-3-benzenesulfonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
0.024
(S)-3-benzenesulfonylamino-4-oxo-9-phenyl-nonanoic acid
-
-
0.025
(S)-3-benzyloxycarbonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
0.119
(S)-3-benzyloxycarbonylamino-4-oxo-9-phenyl-nonanoic acid
-
-
0.0094
(S)-3-benzynesulfonylamino-4-oxo-butyric acid
-
-
0.119
3-([(benzyloxy)carbonyl]amino)-4-oxo-9-phenylnonanoic 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
-
-
0.083
acetyl-Ala-Pro-Nle-Asp-aldehyde
-
pH 7.5
0.000015
acetyl-DEVD-aldehyde
-
pH 7.5
0.000018
acetyl-DEVD-aldehyde
-
pH 7.5, 25C
0.00002
acetyl-DEVS-aldehyde
-
pH 7.5, 37C
0.000011
acetyl-Tyr-Val-Ala-Asp-CO-(CH2)5-Ph
-
pH 7.5
0.000000056
acetyl-WEHD-aldehyde
-
pH 7.5, 25C
0.00000076
acetyl-YVAD-aldehyde
-
pH 7.5, 25C
0.000001
acetyl-YVAD-aldehyde
-
pH 7.5, 37C
0.000006
acetyl-YVAD-aldehyde
-
pH 7.5
0.03
benzyloxycarbonyl-Pro-Nle-Asp-aldehyde
-
pH 7.5
-
0.000008
benzyloxycarbonyl-VAD-CHO
-
-
0.00000001
cowpox serpin CrmA
-
pH 7.5, 25C
-
0.00036
Glu-Val-Asp-aldehyde
-
pH 7.5
0.3
kaempferol
-
pH not specified in the publication, 30C, value above
0.014
myricetin
-
pH not specified in the publication, 30C
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 30C
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 30C
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 30C
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 30C
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 30C
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 30C
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 30C
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 30C
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 30C
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 30C
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
0.3
quercetin
-
pH not specified in the publication, 30C, value above
0.118
luteolin
-
pH not specified in the publication, 30C
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
-
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
-
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
-
-
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
-
-
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
-
-
0.0007
1-([2-[(2,6-dimethoxyphenyl)carbonyl]hydrazino]carbonyl)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]cyclohexanecarboxamide
-
-
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
-
-
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
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
-
-
0.000029
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
-
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
0.00001
L-Tyr-L-Val-L-Ala-L-Asp-CHO
-
-
0.0000216
L-Tyr-L-Val-L-Ala-L-Asp-CN
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
0.00024
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
-
-
0.0002
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
-
-
0.00043
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
-
-
0.00049
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
-
-
0.00031
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
0.0029
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-naphthoyl)hydrazino]carbonyl]cyclopropanecarboxamide
-
-
0.00026
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methoxybenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
0.00015
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
0.00058
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(4-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
0.00005
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
0.00005
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
-
-
0.0004
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
-
-
0.00024
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
0.00009
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
-
-
0.00015
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
-
-
0.00043
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)-2,3-dihydro-1H-indene-2-carboxamide
-
-
0.00004
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
-
-
0.00003
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
-
-
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
-
-
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
-
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.000000023
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
0.00000258
NCGC00183681
-
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
-
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
0.0000005
p35
P89116
IC50: 0.5 nM
-
0.0000036
pralnacasan
-
-
0.000000204
VRT-043198
-
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
0.000024
YN-1234
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
-
assay at
7.5
-
hydrolysis of acetyl-WEHD-7-amido-4-methylcoumarin
7.5
B6EEC1
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
37
B6EEC1
assay at
37
-
assay at
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
bacterial infection leads to a decrease in the mRNA levels of caspase-1
Manually annotated by BRENDA team
P29452
low activity
Manually annotated by BRENDA team
-
inhibition of caspase-1 in rat brain reduces spontaneous nonrapid eye movement sleep and nonrapid eye movement sleep enhancement induced by lipopolysaccharide
Manually annotated by BRENDA team
-
functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
Manually annotated by BRENDA team
Mus musculus BALB/cJ
-
recombinant enzyme
-
Manually annotated by BRENDA team
-
from peripheral blood
Manually annotated by BRENDA team
Mus musculus BALB/c
-
-
-
Manually annotated by BRENDA team
-
high activity. Bacterial infection leads to a decrease in the mRNA levels of caspase-1
Manually annotated by BRENDA team
P29452
low activity
Manually annotated by BRENDA team
Mus musculus C3H/An
-
low activity
-
Manually annotated by BRENDA team
A9Q0J3
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
Manually annotated by BRENDA team
-
macrophage-like cells
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
P29452
low activity
Manually annotated by BRENDA team
-
bacterial infection leads to a decrease in the mRNA levels of caspase-1
Manually annotated by BRENDA team
Mus musculus C3H/An
-
low activity
-
Manually annotated by BRENDA team
-
caspase-1 gene is expressed in 1 day post-hatching larvae and its mRNA levels increases throughout development
Manually annotated by BRENDA team
-
primary leukocyte
Manually annotated by BRENDA team
P29452
low activity
Manually annotated by BRENDA team
-
low activity. Bacterial infection leads to a decrease in the mRNA levels of caspase-1
Manually annotated by BRENDA team
Mus musculus C3H/An
-
low activity
-
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
-
-
Manually annotated by BRENDA team
-
bone marrow-derived
Manually annotated by BRENDA team
-
bone-marrow-derived
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
bone-marrow derived
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
Manually annotated by BRENDA team
-
IFN regulatory factor IRF-2(-/-) macrophages exhibit increased basal and gliotoxin-induced caspase-1 mRNA expression and enhanced caspase-1 activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
bone marrow-derived macrophage, BMDM cell
Manually annotated by BRENDA team
-
bone marrow-derived macrophages, wild-type and superoxide dismutase-deficient
Manually annotated by BRENDA team
-
macrophage-like J774.1 cells
Manually annotated by BRENDA team
-
wild-type and TLR4 knockout macrophage
Manually annotated by BRENDA team
Mus musculus C57BL/6
-
bone marrow-derived
-
Manually annotated by BRENDA team
Mus musculus BALB/cJ
-
bone marrow-derived macrophage, BMDM cell
-
Manually annotated by BRENDA team
Mus musculus C57/Bl
-
-
-
Manually annotated by BRENDA team
-
from peripheral blood
Manually annotated by BRENDA team
-
both the active and the precursor domains of caspase-1are localized in the cytoplasmatic matrix and on the cell surface
Manually annotated by BRENDA team
-
primary neuron, caspase-1 is an upstream positive regulator of caspase-6-mediated cell death in primary human neurons
Manually annotated by BRENDA team
-
caspase-1 activity is required for neuronal differentiation of PC12 cells
Manually annotated by BRENDA team
-
bacterial infection leads to a decrease in the mRNA levels of caspase-1
Manually annotated by BRENDA team
-
fibrobalst cell
Manually annotated by BRENDA team
P29452
low activity
Manually annotated by BRENDA team
Mus musculus C3H/An
-
low activity
-
Manually annotated by BRENDA team
-
caspase-1 is increased in lesional psoriatic skin capared with non-lesional psoriatic skin
Manually annotated by BRENDA team
-
bacterial infection leads to a decrease in the mRNA levels of caspase-1
Manually annotated by BRENDA team
Mus musculus C3H/An
-
-
-
Manually annotated by BRENDA team
P29452
low activity
Manually annotated by BRENDA team
-
quantification of caspase-1 p20 subunit levels in culture supernatants of THP-1 cells
Manually annotated by BRENDA team
-
high activity. Bacterial infection leads to a decrease in the mRNA levels of caspase-1
Manually annotated by BRENDA team
-
high activity in from peripheral blood of mevalonate kinase deficiency patients
Manually annotated by BRENDA team
additional information
-
nonmyeloid cell
Manually annotated by BRENDA team
additional information
-
caspase-1 activity is not detected in Jurkat cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
inactive pro-caspase-1
Manually annotated by BRENDA team
-
active mature enzyme
-
Manually annotated by BRENDA team
-
the enzyme is secreted by macrophages
-
Manually annotated by BRENDA team
-
inactive proenzyme
Manually annotated by BRENDA team
Mus musculus C57/Bl
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 10000-20000, activated processed enzyme
?
B6EEC1
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
?
-
x * 45000, inactive zymogen, SDS-PAGE
?
-
x * 45000, pro-caspase-1, SDS-PAGE
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
the activation site in caspase is WFKD (P4,P3,P2,P1)
proteolytic modification
-
activation of pro-caspase-1
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
-
activation of pro-caspase-1
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
-
activation of pro-caspase-1
proteolytic modification
-
pro-caspase-1 is a 45 kDa molecule that autocatalyzes to form active caspase-1
proteolytic modification
P89116
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
additional information
-
caspase-1 is gluthathionylated
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 4C 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
-
crystallographic study of an enzyme inhibitor complex
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap FF column chromatography
-
recombinant caspase-1 solubilized from insoluble inclusion bodies from Escherichi coli by cation exchange chromatography
-
recombinant enzyme
-
recombinant T7-tagged enzyme
-
recombinant His-tagged enzyme by metal affinity chromatography
B6EEC1
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and sequencing of ICE-related cDNAs encoding hybrid caspase-1/caspase-13-like propeptides
Q9MZV7
cloning and sequencing of ICE-related cDNAs encoding hybrid caspase-1/caspase-13-like propeptides
Q9MZV6
caspase-1 expression in Escherichi coli in insoluble inclusion body
-
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 sequence analysis
-
expressed in baculovirus infected insect cells as 30000 Da proteins lacking the propeptide, automaturation into p20 and p10 subunits
-
expressed in COS-1 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
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
-
expression of wild-type and mutant enzymes in HEK-293T cells
-
monocyte expression analysis by quantitative real-time RT-PCR
-
the caspase-1 gene maps on chromosome 11
-
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
-
DNA sequence analysis
-
-
P29452
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
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DNA sequence analysis
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transient transfection of HEK-293 cells with the caspase-1-V5/His fusion protein
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Q9N2I1
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
B6EEC1
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an approximately 32fold increase in caspase-1 expression is observed in the p53-knockin cell line H273
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caspase 1 activity is inhibited in mice lacking active cysteine proteases
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caspase-1 is upregulated in CD8+ cells with decreased expression of interleukin-4 and interleukin-10
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the activation of caspase-1 is markedly inhibited with increasing concentrations of extracellular KCl
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macrophages from A/J mice exhibit reduced caspase-1 activation and IL-1beta secretion compared to C57BL/6 macrophages
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interferon-beta is not required for the activation of caspase-1
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C136S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C169S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C244S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C270S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C285S
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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
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C331S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C362S
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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
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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
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C397S
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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
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C72S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
C77S
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the mutant enzyme shows decreased activity compared to the wild-type enzyme
D297A
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site-directed mutagenesis, mutation at the D297 residue abolishes the effect of caspase-1 on RIG-I
D316A
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site-directed mutagenesis, mutation at the D316 residue does not abolish the effect of caspase-1 on RIG-I
D336A
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site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
E390A
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site-directed mutagenesis, the mutant shows an about 130fold loss of catalytic efficiency compared to the wild-type enzyme
N337A
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site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
R286A
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site-directed mutagenesis, the mutant shows an about 230fold loss of catalytic efficiency compared to the wild-type enzyme
R286K
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site-directed mutagenesis, the mutant shows an about 150fold loss of catalytic efficiency compared to the wild-type enzyme
R286K/E390D
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site-directed mutagenesis, the mutant shows an about 37fold loss of catalytic efficiency compared to the wild-type enzyme
S332A
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site-directed mutagenesis, the mutant shows an about 4fold loss of catalytic efficiency compared to the wild-type enzyme
S333A
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site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
S339A
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site-directed mutagenesis, the mutant shows an about 7fold loss of catalytic efficiency compared to the wild-type enzyme
T334A
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site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
T388A
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site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
additional information
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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
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caspase-1-deficient macrophages show only slightly reduced ATP-triggered MHC-II secretion, overview
additional information
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caspase-1-deficient mice have unimpaired inflammatory responses to necrotic cells
additional information
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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
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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
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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
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secretion of interleukin-1beta following KIM5 infection is reduced in caspase-1-deficient macrophages compared to wild-type macrophages
additional information
Mus musculus C57BL/6
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caspase-1-deficient macrophages show only slightly reduced ATP-triggered MHC-II secretion, overview, 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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additional information
B6EEC1
RNAi silencing
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant caspase-1 from Escherichi coli expressed in insoluble inclusion bodies
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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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
medicine
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ICE activity is a possible target for fighting excessive inflammatory conditions