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Information on EC 3.4.22.36 - caspase-1 and Organism(s) Homo sapiens and UniProt Accession P29466

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.36 caspase-1
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P29466 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-/-
Synonyms
caspase-1, caspase 1, casp1, effector caspase, procaspase-1, interleukin-1beta-converting enzyme, interleukin-1 beta converting enzyme, interleukin-1beta converting enzyme, csp-1, il-1beta-converting enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
apoptosis-related cysteine protease
-
interleukin 1, beta, convertase
-
interleukin-1 converting enzyme
-
C14.001
-
-
-
-
CASP-1
Casp1
-
-
caspase 1
-
-
caspase-1
-
-
Csp-1
-
-
cysteine aspartyl protease-1
-
-
IL-1 beta converting enzyme
-
-
-
-
IL-1 converting enzyme
-
-
IL-1-converting enzyme
-
-
IL-1B converting enzyme
-
-
IL-1BC
-
-
-
-
IL-1beta-converting enzyme
-
-
IL1beta-converting enzyme
-
-
interleukin converting enzyme
-
-
interleukin-1 beta converting enzyme
-
-
-
-
interleukin-1 converting enzyme
-
-
interleukin-1B converting enzyme
-
-
interleukin-1beta converting enzyme
-
-
interleukin-1beta-converting enzyme
-
-
-
-
interleukin-converting enzyme
-
-
p45
-
-
-
-
procaspase-1
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
122191-40-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-acetyl-WEHD-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-WEHD + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
poly(ADP-ribose)polymerase + H2O
?
show the reaction diagram
-
-
-
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
cleavage to the mature interleukin-1beta
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
show the reaction diagram
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
show the reaction diagram
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
-
-
?
succinyl-YVAD-4-nitroanilide + H2O
succinyl-YVAD + 4-nitroaniline
show the reaction diagram
-
-
-
?
(Z-LEHD)2-R110 tetrapeptide + H2O
?
show the reaction diagram
-
-
-
-
?
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-LEVD-4-nitroanilide + H2O
acetyl-LEVD + 4-nitroaniline
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-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
-
-
-
-
?
ataxin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
Bap31 protein + H2O
?
show the reaction diagram
-
-
-
-
?
Bcl-xL + H2O
?
show the reaction diagram
-
-
-
-
?
beta-actin + H2O
?
show the reaction diagram
-
-
-
-
?
calpastatin + H2O
?
show the reaction diagram
-
-
-
-
?
caspase-1 + H2O
?
show the reaction diagram
-
-
-
-
?
DNA replication licensing factor MCM4 + H2O
?
show the reaction diagram
-
-
-
-
?
epidermal growth factor receptor + H2O
?
show the reaction diagram
eukaryotic translation initiation factor 3 subunit J + H2O
?
show the reaction diagram
-
-
-
-
?
GADPH + H2O
?
show the reaction diagram
-
-
-
-
?
gasdermin D + 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
-
-
-
-
?
LMNA Isoform + H2O
?
show the reaction diagram
-
-
-
-
?
MAP-tau Isoform + H2O
?
show the reaction diagram
-
-
-
-
?
MyD88 adaptor-like + H2O
?
show the reaction diagram
Nedd4 + H2O
?
show the reaction diagram
-
-
-
-
?
parkin + H2O
?
show the reaction diagram
PARP + H2O
?
show the reaction diagram
-
-
-
-
?
PLA2G4A + H2O
?
show the reaction diagram
-
-
-
-
?
PPARgamma + H2O
?
show the reaction diagram
-
-
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
pro-caspase-7 + H2O
caspase-7 + ?
show the reaction diagram
-
activation
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
pro-interleukin-18 + H2O
interleukin-18 propeptide
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
pro-interleukin-33 + H2O
interleukin-33 + ?
show the reaction diagram
PSEN1 + H2O
?
show the reaction diagram
-
-
-
-
?
PSEN2 + H2O
?
show the reaction diagram
-
-
-
-
?
pyrin + 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
-
-
-
-
?
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
-
-
-
-
?
TF AP-2alpha + H2O
?
show the reaction diagram
-
-
-
-
?
Trp-Glu-His-Asp-p-nitroanilide + H2O
Trp-Glu-His-Asp + p-nitroaniline
show the reaction diagram
-
-
-
-
?
WEDH + H2O
?
show the reaction diagram
-
-
-
-
?
zyxin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pro-interleukin-18 + H2O
mature interleukin-18 + ?
show the reaction diagram
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
show the reaction diagram
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
-
-
-
?
Bap31 protein + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
MyD88 adaptor-like + H2O
?
show the reaction diagram
parkin + H2O
?
show the reaction diagram
-
cleavage at Asp126-Ser127. Caspase-1 and caspase-8 dependent parkin cleavage in sporadic Parkinson‘s 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
pro-caspase-7 + H2O
caspase-7 + ?
show the reaction diagram
-
activation
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
pro-interleukin-18 + H2O
interleukin-18 propeptide
show the reaction diagram
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
show the reaction diagram
pro-interleukin-1beta + H2O
interleukin-1beta + ?
show the reaction diagram
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
show the reaction diagram
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
show the reaction diagram
pro-interleukin-33 + H2O
interleukin-33 + ?
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
-
-
?
sphingosine kinase 2 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-DEVD-aldehyde
-
acetyl-YVAD-aldehyde
-
acetyl-YVAD-CHO
caspase-1 specific inhibitor
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
irreversible active site inhibitor
Glu-Val-Asp-aldehyde
-
(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
-
-
4-hydroxy-4,5-dicarboxypentadecanoic acid
-
-
5-([benzyl(dihydroxy)-lambda4-sulfanyl]amino)-3-([(benzyloxy)carbonyl]amino)-4-oxopentanoic acid
-
-
Ac-WEHD-CHO
-
active-site inhibitor
Ac-YVAD-chloromethylketone
-
inhibition of caspase-1 with Ac-YVAD-CMK prevents SphK2 cleavage
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-chloromethylketone
-
-
acetyl-Tyr-Val-Ala-Asp-CO-(CH2)5-Ph
-
-
acetyl-WEHD-aldehyde
-
-
acetyl-YVAD-aldehyde
-
-
benzyloxycarbonyl-Pro-Nle-Asp-aldehyde
-
-
benzyloxycarbonyl-VAD-CHO
-
-
benzyloxycarbonyl-VAD-fluoromethylketone
-
t1/2 at 0.001 mM is 2.5 s
benzyloxycarbonyl-YVAD-fluoromethylketone
-
-
berkedrimane A
-
-
berkedrimane B
-
-
carbobenzoxy-L-valyl-L-alanyl-L-aspartyl-[O-methyl]-fluoromethylketone
-
caspase-1-specific inhibitor
carbobenzoxy-valylalanyl-aspartyl-fluoromethylketone
-
-
carbobenzyloxy-Trp-Glu-His-Asp-fluoromethylketone
-
-
carbobenzyloxy-VAD-fluoromethyl ketone
-
pan-caspase inhibitor
carbobenzyloxy-WEHD-fluoromethyl ketone
-
caspase-1-specific inhibitor
cowpox serpin CrmA
-
-
-
CrmA protein
-
-
-
DEVD-fluoromethylketone
-
-
Disulfiram
-
inhibits the enzyme
geranylgeranyl diphosphate
-
the isoprenyl intermediate of non-sterol isoprenoid biosynthesis blocks activation of caspase-1
IDN-6556
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-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
-
-
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-acetyl-YVAD-CHO
-
-
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
pralnacasan
quercetin
-
-
ritonavir
-
blocks caspase-1 activation and inhibits the enzyme
secospiculisporic acid
-
-
serpin proteinase inhibitor 9
-
endogenous inhibitor of caspase-1 activity in human vascular smooth muscle cells
-
spiculisporic acid
-
-
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
Val-Ala-Asp
-
-
VRT-043198
-
-
YN-1234
-
i.e. N-2-naphthoyl-L-valyl-N-[(1S)-2-carboxy-1-formylethyl]-L-prolinamide
YVAD
-
-
YVAD-chloromethylketone
-
-
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
Z-WEHD-fluoromethylketone
-
-
Z-YVAD-fluoromethylketone
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
lipopolysaccharide
-
-
monosodium urate
-
-
-
NLRC4 inflammasome
-
-
-
NLRP1 inflammasome
-
-
-
NLRP3 inflammasome
-
-
-
poly(dA-dT)
-
-
-
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
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000134
4-[[4'-(dimethylamino)phenyl]azo]-benzoic acid-YVADAPV-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
pH 7.5
0.0000115
acetyl-YVAD-7-amido-4-methylcoumarin
pH 7.5
0.000004
pro-interleukin-1beta
pH 7.5
-
0.0000215
succinyl-YVAD-4-nitroanilide
pH 7.5
0.045
acetyl-DQMD-4-nitroanilide
-
pH 7.5, 30°C
0.0085 - 0.018
acetyl-LEVD-4-nitroanilide
0.046
acetyl-VEID-4-nitroanilide
-
pH 7.5, 30°C
0.12
acetyl-VQVD-4-nitroanilide
-
pH 7.5, 30°C
0.004
acetyl-WEHD-7-amido-4-methylcoumarin
-
pH 7.5
0.0073
acetyl-YEVD-4-nitroanilide
-
pH 7.5, 30°C
0.105
acetyl-YEVDGW-amide
-
pH 7.5, 30°C
0.023
acetyl-YVAD-4-nitroanilide
-
pH 7.5, 30°C
0.006
succinyl-YVAD-4-nitroanilide
-
pH 7.5, 37°C
0.02
succinyl-YVAD-7-amido-4-methylcoumarin
-
pH 7.5, 37°C
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 hide
LITERATURE
IMAGE
0.41
4-[[4'-(dimethylamino)phenyl]azo]-benzoic acid-YVADAPV-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid
pH 7.5
1
acetyl-YVAD-7-amido-4-methylcoumarin
pH 7.5
1.2
pro-interleukin-1beta
pH 7.5
-
1.6
succinyl-YVAD-4-nitroanilide
pH 7.5
13
acetyl-WEHD-7-amido-4-methylcoumarin
-
pH 7.5
1
succinyl-YVAD-4-nitroanilide
-
pH 7.5, 37°C
0.35
succinyl-YVAD-7-amido-4-methylcoumarin
-
pH 7.5, 37°C
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000015
acetyl-DEVD-aldehyde
pH 7.5
0.000006
acetyl-YVAD-aldehyde
pH 7.5
0.00036
Glu-Val-Asp-aldehyde
pH 7.5
0.000054
(3S)-3-((6-[((4-[(6-chloropyrazin-2-yl)amino]phenyl)carbonyl)amino]-2-thiophen-2-ylhexanoyl)amino)-4-oxobutanoic acid
-
-
0.000005
(3S)-3-((6-[((4-[(6-methylquinoxalin-2-yl)amino]phenyl)carbonyl)amino]-2-thiophen-2-ylhexanoyl)amino)-4-oxobutanoic acid
-
-
0.000008
(3S)-3-([2-(2-fluorophenyl)-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)-4-oxobutanoic acid
-
-
0.000016
(3S)-3-([2-ethyl-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)-4-oxobutanoic acid
-
-
0.000004
(3S)-3-([6-(([3-methyl-4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)-4-oxobutanoic acid
-
-
0.000005
(3S)-4-oxo-3-([2-phenyl-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.0052
(3S)-4-oxo-3-([4-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)butanoyl]amino)butanoic acid
-
-
0.0028
(3S)-4-oxo-3-([5-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)pentanoyl]amino)butanoic acid
-
-
0.0001
(3S)-4-oxo-3-([6-(([4-(pyrazin-2-ylamino)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
0.037
(3S)-4-oxo-3-([6-(([4-(pyrazin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.00019
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.000043 - 0.00032
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
0.0024
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.000005 - 0.0026
(3S)-4-oxo-3-([7-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)heptanoyl]amino)butanoic acid
0.0001
(3S)-4-oxo-3-[((4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]phenyl)carbonyl)amino]butanoic acid
-
-
0.00026
(3S)-4-oxo-3-[((4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)carbonyl)amino]butanoic acid
-
-
0.001
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]-2,3-dihydropyrazin-2-yl)carbonyl)amino]butanoic acid
-
-
0.0021
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]furan-2-yl)carbonyl)amino]butanoic acid
-
-
0.00012
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)acetyl)amino]butanoic acid
-
-
0.000035
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)carbonyl)amino]butanoic acid
-
-
0.00012
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-3-yl)carbonyl)amino]butanoic acid
-
-
0.000005
(3S)-4-oxo-3-[((6-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]pyridin-3-yl)carbonyl)amino]butanoic acid
-
-
0.00195
(3S)-4-oxo-3-[((trans-4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]cyclohexyl)carbonyl)amino]butanoic acid
-
-
0.0021
(3S)-4-oxo-3-[(7-oxo-7-([4-(quinoxalin-2-ylamino)phenyl]amino)heptanoyl)amino]butanoic acid
-
-
0.0072
(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 30°C
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
0.000018
acetyl-DEVD-aldehyde
-
pH 7.5, 25°C
0.00002
acetyl-DEVS-aldehyde
-
pH 7.5, 37°C
0.000011
acetyl-Tyr-Val-Ala-Asp-CO-(CH2)5-Ph
-
pH 7.5
0.000000056
acetyl-WEHD-aldehyde
-
pH 7.5, 25°C
0.00000076 - 0.000001
acetyl-YVAD-aldehyde
0.03
benzyloxycarbonyl-Pro-Nle-Asp-aldehyde
-
pH 7.5
0.000008
benzyloxycarbonyl-VAD-CHO
-
-
0.00000001
cowpox serpin CrmA
-
pH 7.5, 25°C
-
0.3
kaempferol
-
pH not specified in the publication, 30°C, value above
0.118
luteolin
-
pH not specified in the publication, 30°C
0.014
myricetin
-
pH not specified in the publication, 30°C
0.05
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2R)-1-carboxy-5-phenylpentan-2-yl]-L-alaninamide
-
IC50 above 0.05 mM, in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.0006
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-(benzylamino)-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000945
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-(cyclohexylamino)propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.0012
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(2-fluorobenzyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000965
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(2-methoxybenzyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00137
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(4-hydroxybenzyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000128
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[methyl(phenyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00029
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[(1,3-benzodioxol-5-ylmethyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00182
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[(4-carbamoylbenzyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00189
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[benzyl(methyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000004
N-([4-(quinoxalin-2-ylamino)phenyl]carbonyl)-L-valyl-N-[(1S)-2-carboxy-1-formylethyl]-L-alaninamide
-
-
0.000004
N-acetyl-L-tyrosyl-alpha-glutamyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
0.000014
N-acetyl-L-tyrosylvalyl-N-[1-(carboxymethyl)-2-oxo-7-phenylheptyl]-L-alaninamide
-
-
0.0000239
N-[(benzyloxy)carbonyl]-alpha-glutamyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
0.000004
N-[(benzyloxy)carbonyl]valyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
0.0000004
NCGC00183434
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.3
quercetin
-
pH not specified in the publication, 30°C, value above
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 hide
LITERATURE
IMAGE
0.0000036
(1S,9S)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-9-[(isoquinolin-1-ylcarbonyl)amino]-6,10-dioxooctahydro-6H-pyridazino[1,2-a][1,2]diazepine-1-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.000004
(3S)-3-[([(1S,9S)-9-[(isoquinolin-1-ylcarbonyl)amino]-6,10-dioxooctahydro-6H-pyridazino[1,2-a][1,2]diazepin-1-yl]carbonyl)amino]-4-oxobutanoic acid
Homo sapiens
-
-
0.000004
(3S)-3-[([(3S,6S,9aR)-6-[(isoquinolin-1-ylcarbonyl)amino]-5-oxo-2,3,5,6,9,9a-hexahydro-1H-pyrrolo[1,2-a]azepin-3-yl]carbonyl)amino]-4-oxobutanoic acid
Homo sapiens
-
-
0.000003
(3S)-3-[([(4S,7S,10aS)-7-[(isoquinolin-1-ylcarbonyl)amino]-6-oxo-3,4,6,7,10,10a-hexahydro-1H-[1,4]oxazino[4,3-a]azepin-4-yl]carbonyl)amino]-4-oxobutanoic acid
Homo sapiens
-
-
0.0007
1-([2-[(2,6-dimethoxyphenyl)carbonyl]hydrazino]carbonyl)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000007 - 0.000015
2,5-dichloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
0.000008 - 0.000029
3-chloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
0.000015
acetyl-L-Leu-L-Glu-L-His-L-Asp-CHO
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.1
berkedrimane A
Homo sapiens
-
at 37°C, pH not specified in the publication
0.09
berkedrimane B
Homo sapiens
-
at 37°C, pH not specified in the publication
0.00001
L-Tyr-L-Val-L-Ala-L-Asp-CHO
Homo sapiens
-
-
0.0000216
L-Tyr-L-Val-L-Ala-L-Asp-CN
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.000001
N-((S,Z)-1-((R)-1-((3S)-2-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
Homo sapiens
-
-
0.000013
N-((S,Z)-1-((S)-1-((3S)-2-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
Homo sapiens
-
-
0.00002
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-1-benzothiophene-2-carboxamide
Homo sapiens
-
-
0.000011
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-3-(trifluoromethyl)benzamide
Homo sapiens
-
-
0.000053
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-3-methoxybenzamide
Homo sapiens
-
-
0.000168
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
0.000027
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]isoquinoline-1-carboxamide
Homo sapiens
-
-
0.000014
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000002
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-6-[[(phenylcarbonyl)amino]methyl]-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000003
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-6-[[(phenylsulfonyl)amino]methyl]-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000002
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(2-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000001
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(3-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000001
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(4-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000019
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-methyl-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.00024
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
Homo sapiens
-
-
0.0002
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
Homo sapiens
-
-
0.00043
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
Homo sapiens
-
-
0.00049
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
Homo sapiens
-
-
0.00031
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.0029
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-naphthoyl)hydrazino]carbonyl]cyclopropanecarboxamide
Homo sapiens
-
-
0.00026
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methoxybenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00015
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00058
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(4-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00005
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00005
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.0004
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
Homo sapiens
-
-
0.00024
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00009
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.00015
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
Homo sapiens
-
-
0.00043
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)-2,3-dihydro-1H-indene-2-carboxamide
Homo sapiens
-
-
0.00004
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
Homo sapiens
-
-
0.00003
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
Homo sapiens
-
-
0.000022
N-[(3S)-6-(hydroxymethyl)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000077
N-[(3S,5Z)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-1,2,3,4,7,8-hexahydroazocin-3-yl]isoquinoline-1-carboxamide
Homo sapiens
-
-
0.00032
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]-1-benzothiophene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.0023
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]benzamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00013
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]isoquinoline-1-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00015
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]naphthalene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00008
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]-1-benzothiophene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
9
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]-3-(trifluoromethyl)benzamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00035
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]benzamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00007
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]isoquinoline-1-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00003
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]naphthalene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.000000023
NCGC00183434
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.00000258
NCGC00183681
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.0000434
NCGC00185682
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.0000036
pralnacasan
Homo sapiens
-
-
0.000000204
VRT-043198
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.000024
YN-1234
Homo sapiens
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
7.5
-
hydrolysis of acetyl-WEHD-7-amido-4-methylcoumarin
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
from peripheral blood
Manually annotated by BRENDA team
-
high activity in from peripheral blood of mevalonate kinase deficiency patients
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 is increased in lesional psoriatic skin capared with non-lesional psoriatic skin
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 hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
caspase-1 is a proinflammatory enzyme that plays pivotal roles in innate immunity and many inflammatory conditions such as periodic fever syndromes and gout
malfunction
-
release of truncated SphK2 into the supernatant is attenuated in caspase-1 knockdown cells
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CASP1_HUMAN
404
0
45159
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10244
1 * 19844 + 1 * 10244, calculated from amino acid sequence
19844
1 * 19844 + 1 * 10244, calculated from amino acid sequence
45000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
1 * 19844 + 1 * 10244, calculated from amino acid sequence
monomer or dimer
mature caspase-1 exists predominantly as a monomer under physiological concentration that undergoes dimerization in the presence of substrate
additional information
-
structure of the on-state and the off-state of caspase-1, four of the network H-bonding side chains, Ser332, Ser333, Ser339, and Thr388, form a cluster that lies behind loop 2, consisting of residues 285-290, which contains the catalytic Cys285
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
additional information
-
caspase-1 is gluthathionylated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallographic study of an enzyme inhibitor complex
enzyme mutants in complex with 3-[2-(2-benzyloxycarbonylamino-3-methyl-butyrylamino)-propionylamino]-4-oxo-pentanoic acid, hanging drop vapor diffusion method, using 0.1 M PIPES pH 6.0, 75-175 mM (NH4)2SO4, 25% (w/v) PEG 2000 MME, 10 mM dithiothreitol, 3 mM NaN3, and 2 mM MgCl2
active forms of caspase-1 bound to the active-site inhibitors Ac-WEHD-CHO and z-Val-Ala-Asp-fluoromethylketone, or active-site ligand-free enzyme, the active-site ligand-free and allosterically inhibited conformations are nearly identical, hanging-drop vapor diffusion at 4°C against a reservoir containing for mutant R286K: 0.1 M 1,4-piperazinediethanesulfonic acid, pH 6.0, 200 mM Li2SO4, 25% PEG 2000 MME, 10 mM DTT, 3 mM NaN3, and 2 mM MgCl2, or for mutant E390D: 0.1 M Pipes, pH 6.0, 350 mM (NH4)2SO4, 20% PEG 2000 MME, 10 mM DTT, 3 mM NaN3, and 2 mM MgCl2, or for mutant R286K/E390D: 0.1 M Pipes, pH 6.0, 175 mM (NH4)2SO4, 20% PEG 2000 MME, 10 mM DTT, 3 mM NaN3, and 2 mM MgCl, X-ray diffraction structure determination and analysis at 1.8-2.1 A resolution, molecular replacement
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A329T
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
C285A
K319R
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
L265S
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
N263S
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
R221C
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
R240Q
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
T267I
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
A329T
-
a procaspase-1 variant with decreased enzymatic activity
C136S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C169S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C244S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C270S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C285A
-
a procaspase-1 variant with decreased enzymatic activity showing about 3.5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
C285S
C331S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C362S
-
the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C362S/C397S
-
the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C364S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C397S
-
the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C69S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C72S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C77S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
D297A
-
site-directed mutagenesis, mutation at the D297 residue abolishes the effect of caspase-1 on RIG-I
D316A
-
site-directed mutagenesis, mutation at the D316 residue does not abolish the effect of caspase-1 on RIG-I
D336A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
E390A
-
site-directed mutagenesis, the mutant shows an about 130fold loss of catalytic efficiency compared to the wild-type enzyme
K319R
-
a procaspase-1 variant with decreased enzymatic activity showing about 1.6fold increased nuclear factor-kappaB activation compared to the wild type enzyme
L265S
-
a procaspase-1 variant with decreased enzymatic activity showing about 6.5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
N263S
-
a procaspase-1 variant with decreased enzymatic activity showing about 1.8fold increased nuclear factor-kappaB activation compared to the wild type enzyme
N337A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
R221C
-
a procaspase-1 variant with decreased enzymatic activity
R240Q
-
a procaspase-1 variant with decreased enzymatic activity showing about 5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
R286A
-
site-directed mutagenesis, the mutant shows an about 230fold loss of catalytic efficiency compared to the wild-type enzyme
R286K
-
site-directed mutagenesis, the mutant shows an about 150fold loss of catalytic efficiency compared to the wild-type enzyme
R286K/E390D
-
site-directed mutagenesis, the mutant shows an about 37fold loss of catalytic efficiency compared to the wild-type enzyme
S332A
-
site-directed mutagenesis, the mutant shows an about 4fold loss of catalytic efficiency compared to the wild-type enzyme
S333A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
S339A
-
site-directed mutagenesis, the mutant shows an about 7fold loss of catalytic efficiency compared to the wild-type enzyme
T267I
-
a procaspase-1 variant with decreased enzymatic activity
T334A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
T388A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap Ni-NTA column chromatography and Superdex 200 gel filtration
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 Codon Plus cells
expressed in Escherichia coli BL21(DE3) Star cells as insoluble inclusion bodies
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an approximately 32fold increase in caspase-1 expression is observed in the p53-knockin cell line H273
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
50 mM HEPES (pH 8.0), 100 mM NaCl, 10% (w/v) sucrose, 1 M nondetergent sulfobetaine 201, and 10 mM dithiothreitol
recombinant caspase-1 from Escherichi coli expressed in insoluble inclusion bodies
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garcia-Calvo, M.; Peterson, E.P.; Leiting, B.; Ruel, R.; Nicholson, D.W.; Thornberry, N.A.
Inhibition of human caspases by peptide-based and macromolecular inhibitors
J. Biol. Chem.
273
32608-32613
1998
Homo sapiens
Manually annotated by BRENDA team
Garcia-Calvo, M.; Peterson, E.P.; Rasper, D.M.; Vaillancourt, J.P.; Zamboni, R.; Nicholson, D.W.; Thornberry, N.A.
Purification and catalytic properties of human caspase family members
Cell Death Differ.
6
362-369
1999
Homo sapiens
Manually annotated by BRENDA team
Chang, H.Y.; Yang, X.
Proteases from cell suicide: functions and regulation of caspases
Microbiol. Mol. Biol. Rev.
64
821-846
2000
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Thornberry, N.A.; Rano, T.A.; Peterson, E.P.; et al.
A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
J. Biol. Chem.
272
17907-17911
1997
Homo sapiens
Manually annotated by BRENDA team
Kahns, S.; Kalai, M.; Jakobsen, L.D.; Clark, B.F.; Vandenabeele, P.; Jensen, P.H.
Caspase-1 and caspase-8 cleave and inactivate cellular parkin
J. Biol. Chem.
278
23376-23380
2003
Homo sapiens
Manually annotated by BRENDA team
Talanian, R.V.; Quinlan, C.; Trautz, S.; Hackett, M.C.; Mankovich, J.A.; Banach, D.; Ghayur, T.; Brady, K.D.; Wong, W.W.
Substrate specificities of caspase family proteases
J. Biol. Chem.
272
9677-9682
1997
Homo sapiens
Manually annotated by BRENDA team
Margolin, N.; Raybuck, S.A.; Wilson, K.P.; Chen, W.; Fox, T.; Gu, Y.; Livingston, D.J.
Substrate and inhibitor specificity of interleukin-1beta-converting enzyme and related caspases
J. Biol. Chem.
272
7223-7228
1997
Homo sapiens (P29466)
Manually annotated by BRENDA team
Pirhonen, J.; Sareneva, T.; Julkunen, I.; Matikainen, S.
Virus infection induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
Eur. J. Immunol.
31
726-733
2001
Homo sapiens
Manually annotated by BRENDA team
Bae, S.S.; Choi, J.H.; Oh, Y.S.; Perry, D.K.; Ryu, S.H.; Suh, P.G.
Proteolytic cleavage of epidermal growth factor receptor by caspases
FEBS Lett.
491
16-20
2001
Homo sapiens
Manually annotated by BRENDA team
Kisselev, A.F.; Garcia-Calvo, M.; Overkleeft, H.S.; Peterson, E.; Pennington, M.W.; Ploegh, H.L.; Thornberry, N.A.; Goldberg, A.L.
the caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites
J. Biol. Chem.
278
35869-35877
2003
Homo sapiens
Manually annotated by BRENDA team
Fassy, F.; Krebs, O.; Rey, H.; Komara, B.; Gillard, C.; Capdevila, C.; Yea, C.; Faucheu, C.; Blanchet, A.M.; Miossec, C.; Diu-Hercend, A.
Enzymic activity of two caspases related to interleukin-1beta-converting enzyme
Eur. J. Biochem.
253
76-83
1998
Homo sapiens
Manually annotated by BRENDA team
Thornberry, N.A.; Bull, H.G.; Calaycay, J.R.; et al.
A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes
Nature
356
768-774
1992
Homo sapiens (P29466)
Manually annotated by BRENDA team
Cerretti, D.P.; Kozlosky, C.J.; Mosley, B.; et al.
Molecular cloning of the interleukin-1 beta converting enzyme
Science
256
97-100
1992
Homo sapiens (P29466), Homo sapiens
Manually annotated by BRENDA team
Walker, N.P.C.; Talanian, R.V.; Brady, K.D.; Dang, L.C.; et al.
Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer
Cell
78
343-352
1994
Homo sapiens (P29466)
Manually annotated by BRENDA team
Okamoto, Y.; Anan, H.; Nakai, E.; Morihira, K.; Yonetoku, Y.; Kurihara, H.; Sakashita, H.; Terai, Y.; Takeuchi, M.; Shibanuma, T.
Isomura, Y.: Peptide based interleukin-1 beta converting enzyme (ICE) inhibitors: synthesis, structure activity relationships and crystallographic study of the ICE-inhibitor complex
Chem. Pharm. Bull.
47
11-21
1999
Homo sapiens (P29466)
Manually annotated by BRENDA team
Alnemri, E.S.; Fernandes-Alnemri, T.; Litwack, G.
Cloning and expression of four novel isoforms of human interleukin-1 beta converting enzyme with different apoptotic activities
J. Biol. Chem.
270
4312-4317
1995
Homo sapiens (P29466), Homo sapiens
Manually annotated by BRENDA team
Young, J.L.; Sukhova, G.K.; Foster, D.; Kisiel, W.; Libby, P.; Schonbeck, U.
The serpin proteinase inhibitor 9 is an endogenous inhibitor of interleukin 1beta-converting enzyme (caspase-1) activity in human vascular smooth muscle cells
J. Exp. Med.
191
1535-1544
2000
Homo sapiens
Manually annotated by BRENDA team
Shahripour, A.B.; Plummer, M.S.; Lunney, E.A.; Albrecht, H.P.; Hays, S.J.; Kostlan, C.R.; Sawyer, T.K.; Walker, N.P.; Brady, K.D.; Allen, H.J.; Talanian, R.V.; Wong, W.W.; Humblet, C.
Structure-based design of nonpeptide inhibitors of interleukin-1beta converting enzyme (ICE, caspase-1)
Bioorg. Med. Chem.
10
31-40
2002
Homo sapiens
Manually annotated by BRENDA team
Harter, W.G.; Albrect, H.; Brady, K.; Caprathe, B.; Dunbar, J.; Gilmore, J.; Hays, S.; Kostlan, C.R.; Lunney, B.; Walker, N.
The design and synthesis of sulfonamides as caspase-1 inhibitors
Bioorg. Med. Chem. Lett.
14
809-812
2004
Homo sapiens
Manually annotated by BRENDA team
Fahr, B.T.; OBrien, T.; Pham, P.; Waal, N.D.; Baskaran, S.; Raimundo, B.C.; Lam, J.W.; Sopko, M.M.; Purkey, H.E.; Romanowski, M.J.
Tethering identifies fragment that yields potent inhibitors of human caspase-1
Bioorg. Med. Chem. Lett.
16
559-562
2006
Homo sapiens
Manually annotated by BRENDA team
Guo, H.; Petrin, D.; Zhang, Y.; Bergeron, C.; Goodyer, C.G.; LeBlanc, A.C.
Caspase-1 activation of caspase-6 in human apoptotic neurons
Cell Death Differ.
13
285-292
2006
Homo sapiens
Manually annotated by BRENDA team
Thalappilly, S.; Sadasivam, S.; Radha, V.; Swarup, G.
Involvement of caspase 1 and its activator Ipaf upstream of mitochondrial events in apoptosis
FEBS J.
273
2766-2778
2006
Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; O'Neil, S.V.; Wos, J.A.; Oppong, K.A.; Laufersweiler, M.C.; Soper, D.L.; Ellis, C.D.; Baize, M.W.; Fancher, A.N.; Lu, W.; Suchanek, M.K.; Wang, R.L.; Schwecke, W.P.; Cruze, C.A.; Buchalova, M.; Belkin, M.; De, B.; Demuth, T.P.
Synthesis and evaluation of unsaturated caprolactams as interleukin-1beta converting enzyme (ICE) inhibitors
Bioorg. Med. Chem.
15
1311-1322
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Soper, D.L.; Sheville, J.; ONeil, S.V.; Wang, Y.; Laufersweiler, M.C.; Oppong, K.A.; Wos, J.A.; Ellis, C.D.; Fancher, A.N.; Lu, W.; Suchanek, M.K.; Wang, R.L.; De, B.; Demuth, T.P.
Synthesis and evaluation of novel 1-(2-acylhydrazinocarbonyl)-cycloalkyl carboxamides as interleukin-1beta converting enzyme (ICE) inhibitors
Bioorg. Med. Chem. Lett.
16
4233-4236
2006
Homo sapiens
Manually annotated by BRENDA team
Ellis, C.D.; Oppong, K.A.; Laufersweiler, M.C.; ONeil, S.V.; Soper, D.L.; Wang, Y.; Wos, J.A.; Fancher, A.N.; Lu, W.; Suchanek, M.K.; Wang, R.L.; De, B.; Demuth, T.P.
Synthesis and evaluation of thiazepines as interleukin-1beta converting enzyme (ICE) inhibitors
Bioorg. Med. Chem. Lett.
16
4728-4732
2006
Homo sapiens
Manually annotated by BRENDA team
Gurcel, L.; Abrami, L.; Girardin, S.; Tschopp, J.; van der Goot, F.G.
Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
Cell
126
1135-1145
2006
Homo sapiens
Manually annotated by BRENDA team
Keller, M.; Rueegg, A.; Werner, S.; Beer, H.D.
Active caspase-1 is a regulator of unconventional protein secretion
Cell
132
818-831
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Adlbrecht, C.; Hoetzenecker, K.; Posch, M.; Steiner, S.; Kopp, C.; Hacker, S.; Auer, J.; Horvath, R.; Moser, B.; Roth, G.; Wolner, E.; Lang, I.M.; Ankersmit, H.J.
Elevated levels of interleukin-1beta-converting enzyme and caspase-cleaved cytokeratin-18 in acute myocardial infarction
Eur. J. Clin. Invest.
37
372-380
2007
Homo sapiens
Manually annotated by BRENDA team
Johansen, C.; Moeller, K.; Kragballe, K.; Iversen, L.
The activity of caspase-1 is increased in lesional psoriatic epidermis
J. Invest. Dermatol.
127
2857-2864
2007
Homo sapiens
Manually annotated by BRENDA team
Miggin, S.M.; Palsson-McDermott, E.; Dunne, A.; Jefferies, C.; Pinteaux, E.; Banahan, K.; Murphy, C.; Moynagh, P.; Yamamoto, M.; Akira, S.; Rothwell, N.; Golenbock, D.; Fitzgerald, K.A.; ONeill, L.A.
NF-kappaB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1
Proc. Natl. Acad. Sci. USA
104
3372-3377
2007
Homo sapiens
Manually annotated by BRENDA team
Kuijk, L.M.; Beekman, J.M.; Koster, J.; Waterham, H.R.; Frenkel, J.; Coffer, P.J.
HMG-CoA reductase inhibition induces IL-1beta release through Rac1/PI3K/PKB-dependent caspase-1 activation
Blood
112
3563-3573
2008
Homo sapiens
Manually annotated by BRENDA team
Chae, J.J.; Wood, G.; Richard, K.; Jaffe, H.; Colburn, N.T.; Masters, S.L.; Gumucio, D.L.; Shoham, N.G.; Kastner, D.L.
The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-kappaB through its N-terminal fragment
Blood
112
1794-1803
2008
Homo sapiens
Manually annotated by BRENDA team
Yu, H.B.; Finlay, B.B.
The caspase-1 inflammasome: a pilot of innate immune responses
Cell Host Microbe
4
198-208
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Roth, G.A.; Faybik, P.; Hetz, H.; Hacker, S.; Ankersmit, H.J.; Bacher, A.; Thalhammer, T.; Krenn, C.G.
Pro-inflammatory interleukin-18 and caspase-1 serum levels in liver failure are unaffected by MARS treatment
Dig. Liver Dis.
41
417-423
2008
Homo sapiens
Manually annotated by BRENDA team
Hurst, J.; Prinz, N.; Lorenz, M.; Bauer, S.; Chapman, J.; Lackner, K.J.; von Landenberg, P.
TLR7 and TLR8 ligands and antiphospholipid antibodies show synergistic effects on the induction of IL-1beta and caspase-1 in monocytes and dendritic cells
Immunobiology
214
683-691
2009
Homo sapiens
Manually annotated by BRENDA team
Kim, M.J.; Yoo, J.Y.
Active caspase-1-mediated secretion of retinoic acid inducible gene-I
J. Immunol.
181
7324-7331
2008
Homo sapiens
Manually annotated by BRENDA team
Gotsch, F.; Romero, R.; Chaiworapongsa, T.; Erez, O.; Vaisbuch, E.; Espinoza, J.; Kusanovic, J.P.; Mittal, P.; Mazaki-Tovi, S.; Kim, C.J.; Kim, J.S.; Edwin, S.; Nhan-Chang, C.L.; Hamill, N.; Friel, L.; Than, N.G.; Mazor, M.; Yoon, B.H.; Hassan, S.S.
Evidence of the involvement of caspase-1 under physiologic and pathologic cellular stress during human pregnancy: a link between the inflammasome and parturition
J. Matern. Fetal. Neonatal. Med.
21
605-616
2008
Homo sapiens
Manually annotated by BRENDA team
Datta, D.; Scheer, J.M.; Romanowski, M.J.; Wells, J.A.
An allosteric circuit in caspase-1
J. Mol. Biol.
381
1157-1167
2008
Homo sapiens
Manually annotated by BRENDA team
da Cunha, J.P.; Galante, P.A.; de Souza, S.J.
Different evolutionary strategies for the origin of caspase-1 inhibitors
J. Mol. Evol.
66
591-597
2008
Homo sapiens, Macaca mulatta, Pan troglodytes
Manually annotated by BRENDA team
Foley, K.; Kast, R.E.; Altschuler, E.L.
Ritonavir and disulfiram have potential to inhibit caspase-1 mediated inflammation and reduce neurological sequelae after minor blast exposure
Med. Hypotheses
72
150-152
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Kuijk, L.M.; Mandey, S.H.; Schellens, I.; Waterham, H.R.; Rijkers, G.T.; Coffer, P.J.; Frenkel, J.
Statin synergizes with LPS to induce IL-1beta release by THP-1 cells through activation of caspase-1
Mol. Immunol.
45
2158-2165
2008
Homo sapiens
Manually annotated by BRENDA team
Franchi, L.; Eigenbrod, T.; Munoz-Planillo, R.; Nunez, G.
The inflammasome: a caspase-1-activation platform that regulates immune responses and disease pathogenesis
Nat. Immunol.
10
241-247
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Meissner, F.; Molawi, K.; Zychlinsky, A.
Superoxide dismutase 1 regulates caspase-1 and endotoxic shock
Nat. Immunol.
9
866-872
2008
Homo sapiens
Manually annotated by BRENDA team
Hornung, V.; Ablasser, A.; Charrel-Dennis, M.; Bauernfeind, F.; Horvath, G.; Caffrey, D.R.; Latz, E.; Fitzgerald, K.A.
AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
Nature
458
514-518
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Giamarellos-Bourboulis, E.; Mouktaroudi, M.; Bodar, E.; Van Der Ven, J.; Kullberg, B.; Netea, M.; Van Der Meer, J.
Crystals of monosodium urate monohydrate enhance lipopolysaccharide-induced release of interleukin 1beta by mononuclear cells through a caspase 1-mediated process
Ann. Rheum. Dis.
68
273-278
2009
Homo sapiens
Manually annotated by BRENDA team
Martin, T.M.; Zhang, Z.; Kurz, P.; Rose, C.D.; Chen, H.; Lu, H.; Planck, S.R.; Davey, M.P.; Rosenbaum, J.T.
The NOD2 defect in Blau syndrome does not result in excess interleukin-1 activity
Arthritis Rheum.
60
611-618
2009
Homo sapiens
Manually annotated by BRENDA team
Morishige, T.; Yoshioka, Y.; Tanabe, A.; Yao, X.; Tsunoda, S.; Tsutsumi, Y.; Mukai, Y.; Okada, N.; Nakagawa, S.
Titanium dioxide induces different levels of IL-1beta production dependent on its particle characteristics through caspase-1 activation mediated by reactive oxygen species and cathepsin B
Biochem. Biophys. Res. Commun.
392
160-165
2010
Homo sapiens
Manually annotated by BRENDA team
Boxer, M.B.; Quinn, A.M.; Shen, M.; Jadhav, A.; Leister, W.; Simeonov, A.; Auld, D.S.; Thomas, C.J.
A highly potent and selective caspase 1 inhibitor that utilizes a key 3-cyanopropanoic acid moiety
ChemMedChem
5
730-738
2010
Homo sapiens
Manually annotated by BRENDA team
Vezzani, A.; Balosso, S.; Maroso, M.; Zardoni, D.; Noe, F.; Ravizza, T.
ICE/caspase 1 inhibitors and IL-1beta receptor antagonists as potential therapeutics in epilepsy
Curr. Opin. Investig. Drugs
11
43-50
2010
Homo sapiens
Manually annotated by BRENDA team
Chopra, P.; Gupta, S.; Dastidar, S.G.; Ray, A.
Development of cell death-based method for the selectivity screening of caspase-1 inhibitors
Cytotechnology
60
77-83
2009
Homo sapiens
Manually annotated by BRENDA team
Cho, M.H.; Ahn, H.J.; Ha, H.J.; Park, J.; Chun, J.H.; Kim, B.S.; Oh, H.B.; Rhie, G.E.
Bacillus anthracis capsule activates caspase-1 and induces interleukin-1beta release from differentiated THP-1 and human monocyte-derived dendritic cells
Infect. Immun.
78
387-392
2010
Homo sapiens
Manually annotated by BRENDA team
Abdul-Sater, A.A.; Koo, E.; Haecker, G.; Ojcius, D.M.
Inflammasome-dependent caspase-1 activation in cervical epithelial cells stimulates growth of the intracellular pathogen Chlamydia trachomatis
J. Biol. Chem.
284
26789-26796
2009
Homo sapiens
Manually annotated by BRENDA team
Okamoto, M.; Liu, W.; Luo, Y.; Tanaka, A.; Cai, X.; Norris, D.A.; Dinarello, C.A.; Fujita, M.
Constitutively active inflammasome in human melanoma cells mediating autoinflammation via caspase-1 processing and secretion of interleukin-1beta
J. Biol. Chem.
285
6477-6488
2010
Homo sapiens
Manually annotated by BRENDA team
Ulrichts, P.; Bovijn, C.; Lievens, S.; Beyaert, R.; Tavernier, J.; Peelman, F.
Caspase-1 targets the TLR adaptor Mal at a crucial TIR-domain interaction site
J. Cell Sci.
123
256-265
2010
Homo sapiens
Manually annotated by BRENDA team
Keller, M.; Sollberger, G.; Beer, H.D.
Thalidomide inhibits activation of caspase-1
J. Immunol.
183
5593-5599
2009
Homo sapiens
Manually annotated by BRENDA team
Loeser, R.; Abbenante, G.; Madala, P.K.; Halili, M.; Le, G.T.; Fairlie, D.P.
Noncovalent tripeptidyl benzyl- and cyclohexyl-amine inhibitors of the cysteine protease caspase-1
J. Med. Chem.
53
2651-2655
2010
Homo sapiens
Manually annotated by BRENDA team
Nasirudeen, A.M.; Liu, D.X.
Gene expression profiling by microarray analysis reveals an important role for caspase-1 in dengue virus-induced p53-mediated apoptosis
J. Med. Virol.
81
1069-1081
2009
Homo sapiens (P29466), Homo sapiens
Manually annotated by BRENDA team
Agard, N.J.; Maltby, D.; Wells, J.A.
Inflammatory stimuli regulate caspase substrate profiles
Mol. Cell. Proteomics
9
880-893
2010
Homo sapiens
Manually annotated by BRENDA team
Sarkar, A.; Mitra, S.; Mehta, S.; Raices, R.; Wewers, M.D.
Monocyte derived microvesicles deliver a cell death message via encapsulated caspase-1
PLoS ONE
4
e7140
2009
Homo sapiens
Manually annotated by BRENDA team
Shen, J.; Yin, Y.; Mai, J.; Xiong, X.; Pansuria, M.; Liu, J.; Maley, E.; Saqib, N.U.; Wang, H.; Yang, X.F.
Caspase-1 recognizes extended cleavage sites in its natural substrates
Atherosclerosis
210
422-429
2010
Homo sapiens
Manually annotated by BRENDA team
Weigert, A.; Cremer, S.; Schmidt, M.V.; von Knethen, A.; Angioni, C.; Geisslinger, G.; Bruene, B.
Cleavage of sphingosine kinase 2 by caspase-1 provokes its release from apoptotic cells
Blood
115
3531-3540
2010
Homo sapiens
Manually annotated by BRENDA team
White, J.; Beckford, J.; Yadegarynia, S.; Ngo, N.; Lialiutska, T.; DAlarcao, M.
Some natural flavonoids are competitive inhibitors of caspase-1, -3, and -7 despite their cellular toxicity
Food Chem.
131
1453-1459
2012
Homo sapiens
Manually annotated by BRENDA team
Narayanan, K.B.; Park, H.H.
Purification and analysis of the interactions of caspase-1 and ASC for assembly of the inflammasome
Appl. Biochem. Biotechnol.
175
2883-2894
2015
Homo sapiens
Manually annotated by BRENDA team
Luksch, H.; Romanowski, M.J.; Chara, O.; Tuengler, V.; Caffarena, E.R.; Heymann, M.C.; Lohse, P.; Aksentijevich, I.; Remmers, E.F.; Flecks, S.; Quoos, N.; Gramatte, J.; Petzold, C.; Hofmann, S.R.; Winkler, S.; Pessler, F.; Kallinich, T.; Ganser, G.; Nimtz-Talaska, A.; Baumann, U.; Runde, V.; Grimbacher, B., et al
Naturally occurring genetic variants of human caspase-1 differ considerably in structure and the ability to activate interleukin-1beta
Hum. Mutat.
34
122-131
2013
Homo sapiens (P29466), Homo sapiens
Manually annotated by BRENDA team
Datta, D.; McClendon, C.L.; Jacobson, M.P.; Wells, J.A.
Substrate and inhibitor-induced dimerization and cooperativity in caspase-1 but not caspase-3
J. Biol. Chem.
288
9971-9981
2013
Homo sapiens (P29466)
Manually annotated by BRENDA team
Heymann, M.C.; Winkler, S.; Luksch, H.; Flecks, S.; Franke, M.; Russ, S.; Ozen, S.; Yilmaz, E.; Klein, C.; Kallinich, T.; Lindemann, D.; Brenner, S.; Ganser, G.; Roesler, J.; Roesen-Wolff, A.; Hofmann, S.R.
Human procaspase-1 variants with decreased enzymatic activity are associated with febrile episodes and may contribute to inflammation via RIP2 and NF-kappaB signaling
J. Immunol.
192
4379-4385
2014
Homo sapiens
Manually annotated by BRENDA team
Sollberger, G.; Strittmatter, G.E.; Grossi, S.; Garstkiewicz, M.; Auf dem Keller, U.; French, L.E.; Beer, H.D.
Caspase-1 activity is required for UVB-induced apoptosis of human keratinocytes
J. Invest. Dermatol.
135
1395-1404
2015
Homo sapiens
Manually annotated by BRENDA team
Stierle, D.B.; Stierle, A.A.; Girtsman, T.; McIntyre, K.; Nichols, J.
Caspase-1 and -3 inhibiting drimane sesquiterpenoids from the extremophilic fungus Penicillium solitum
J. Nat. Prod.
75
262-266
2012
Homo sapiens
Manually annotated by BRENDA team