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Information on EC 3.4.22.56 - caspase-3
for references in articles please use BRENDA:EC3.4.22.56
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.22 Cysteine endopeptidases
3.4.22.56 caspase-3
IUBMB Comments
Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60) . These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype [3,5]. Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B . Caspase-3 can activate procaspase-2 (EC 3.4.22.55) . Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain . Although Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate . Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp┼ is a better substrate than Asp-Val-Ala-Asp┼ . This is not the case for caspase-7 . Belongs in peptidase family C14.
The enzyme appears in viruses and cellular organisms
- 3.4.22.56
- bcl-2
- caspase-9
- necrosis
-
tunel
- parp
-
anti-apoptotic
-
neuroprotective
-
pro-apoptotic
- tnf
- endothelial
-
annexin
- leukemia
-
apoptosis-related
- mapks
- fas
- ischemia
- dismutase
-
deoxynucleotidyl
- erk
-
neurotoxicity
- artery
- cyclin
- cerebral
- dutp
- malondialdehyde
-
reperfusion
- infarct
- nick
- cardiac
- sirna
-
apoptosis-inducing
- myocardial
- gsh
- cardiomyocytes
-
sham
- c-jun
- cisplatin
- survivin
-
transferase-mediated
- iodide
- hippocampal
- adp-ribose
-
hoechst
-
antiproliferative
-
caspase-dependent
-
polyadp-ribose
- bid
-
ischemia-reperfusion
- propidium
-
ladder
- analysis
- drug development
- molecular biology
- medicine
- diagnostics
Reaction Schemes
showstrict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-/- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
Synonyms
caspase-3, caspase 3, casp3, sca-1, cpp32, casp-3, cas-3, cpp-32, apopain, cgcaspase-3, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
apopain
-
-
-
-
C14.003
-
-
-
-
CASP-3
CASP3
caspase 3
CPP-32
-
-
-
-
CPP32
-
-
-
-
CPP32/apopain
-
-
-
-
cysteine aspartic acid-specific protease
cysteine protease CPP32
-
-
-
-
DEVDase
IRP
-
-
-
-
SCA-1
-
-
-
-
SREBP cleavage activity 1
-
-
-
-
Yama protein
-
-
-
-
Yama/CPP32
-
-
-
-
additional information
CASP-3
-
-
-
-
caspase 3
-
-
-
-
additional information
-
the enzyme belongs to the family of cysteine proteases known as caspases
additional information
caspase-3 belongs to the group of executioner caspases of the family of cysteine aspartyl proteases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-/- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-/- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
-
-
-
-
strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-/- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
hydrophobic S5 site, where the side-chains of F250 and F252 interact with substrate. Kinetic importance of P5 site
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
169592-56-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-tetramethylrhodamine-5(6)-carboxamide-DEVD-cyanine 5 + H2O
?
-
Substrates: -
Products: -
Products: -
?
70kDa U1 small ribonucleoprotein + H2O
?
-
Substrates: cleavage site is DGPD-/-
Products: -
Products: -
?
Ac-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
Ac-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Ac-DEVD-4-methylcoumarin 7-amide + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
Substrates: an artificial caspase-3 substrate
Products: -
Products: -
?
Ac-DMQD-4-nitroanilide + H2O
Ac-DMQD + 4-nitroaniline
Substrates: weak substrate
Products: -
Products: -
?
Ac-IETD-4-nitroanilide + H2O
Ac-IETD + 4-nitroaniline
Substrates: an artificial caspase-8 substrate, low activity
Products: -
Products: -
?
Ac-LEHD-4-nitroanilide + H2O
Ac-LEHD + 4-nitroaniline
Substrates: an artificial caspase-9 substrate, low activity
Products: -
Products: -
?
Ac-VDQQD-4-nitroanilide + H2O
Ac-VDQQD + 4-nitroaniline
Substrates: weak substrate
Products: -
Products: -
?
acetyl-Asp-Glu-Val-Asp-4-nitroanilide + H2O
acetyl-Asp-Glu-Val-Asp + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Asp-Glu-Val-Asp-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Asp-Glu-Val-Asp + 7-amino-4-trifluoromethylcoumarin
acetyl-DEVD-4-methylcoumarin-7-amide + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
acetyl-DEVD-4-nitroanilide + H2O
acetyl-DEVD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-DEVD-4-trifluoromethylcoumarin-7-amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
acetyl-DEVD-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-DEVD + 7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
acetyl-DQMD-4-nitroanilide + H2O
acetyl-DQMD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-IETD-7-amido-4-methylcoumarin + H2O
acetyl-IETD + 7-amino-4-methylcoumarin
-
Substrates: low activity towards the caspase-6 and caspase-8 substrate
Products: -
Products: -
?
acetyl-L-Asp-L-Glu-L-Val-L-Asp-4-nitroanilide + H2O
acetyl-L-Asp-L-Glu-L-Val-L-Asp + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin + H2O
acetyl-L-Asp-L-Glu-L-Val-L-Asp + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
acetyl-L-Asp-L-Met-L-Gln-L-Asp-4-nitroanilide + H2O
acetyl-L-Asp-L-Met-L-Gln-L-Asp + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
acetyl-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide + H2O
acetyl-L-Asp-L-Val-L-Ala-L-Asp + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
acetyl-L-Leu-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide + H2O
acetyl-L-Leu-L-Asp-L-Val-L-Ala-L-Asp + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
acetyl-L-Val-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide + H2O
acetyl-L-Val-L-Asp-L-Val-L-Ala-L-Asp + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
acetyl-LEHD-4-methylcoumarin-7-amide + H2O
acetyl-LEHD + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
acetyl-LEHD-7-amido-4-methylcoumarin + H2O
acetyl-LEHD + 7-amino-4-methylcoumarin
-
Substrates: low activity towards the caspase-9 substrate
Products: -
Products: -
?
acetyl-VDQQD-4-nitroanilide + H2O
acetyl-VDQQD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-VDVAD-4-nitroanilide + H2O
acetyl-VAVAD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-VEID-4-methylcoumarin-7-amide + H2O
acetyl-VEID + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
acetyl-VEID-4-nitroanilide + H2O
acetyl-VEID + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-VQVD-4-nitroanilide + H2O
acetyl-VQVD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-YEVD-4-nitroanilide + H2O
acetyl-YEVD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-YVAD-4-nitroanilide + H2O
acetyl-YVAD + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
-
Substrates: low activity towards the caspase-1 substrate
Products: -
Products: -
?
alpha-spectrin + H2O
?
-
Substrates: -
Products: production of a 120 kDa fragment
Products: production of a 120 kDa fragment
?
anamorsin + H2O
?
-
Substrates: specifically cleaved by caspase-3 at DSVD209 L generating 25- and 10-kDa fragments
Products: -
Products: -
?
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin + H2O
benzoyl-L-Asp-L-Glu-L-Val-L-Asp + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-DEVD-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-DEVD + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
benzyloxycarbonyl-VDVAD-7-amido-4-trifluoromethylcoumarin + H2O
benzyloxycarbonyl-VDVAD + 7-amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
beta-catenin + H2O
?
-
Substrates: processing of beta-catenin, production of a 70000 Da fragment
Products: -
Products: -
?
biotinylated acetyl-CDEVDK + H2O
biotinylated acetyl-CDEVD + Lys
-
Substrates: -
Products: -
Products: -
?
caspase 9 + H2O
?
-
Substrates: cleavage by caspase 3 does not result in activation of caspase 9, but enhances apoptosis by alleviating XIAP inhibition of the apical caspase
Products: -
Products: -
?
D4 G-protein dissociation inhibitor + H2O
?
-
Substrates: cleavage site is DELD-/-
Products: -
Products: -
?
D4-GDI(Rho-GDI 2) + H2O
?
-
Substrates: differential regulation of the homologous GDP dissociation inhibitors Rho-GDI 1 and D4-GDI during drug-induced apoptosis by proteolysis mediated by caspase-3
Products: -
Products: -
?
DEVD-7-amido-4-methylcoumarin + H2O
DEVD + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
DEVD-7-amido-4-trifluoromethylcoumarin + H2O
DEVD + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
DEVD-amido-4-trifluoromethylcoumarin + H2O
DEVD + amino-4-trifluoromethylcoumarin
Substrates: -
Products: -
Products: -
?
DEVD-FQ + H2O
N2-acetyl-L-lysyl-L-lysyl-L-lysyl-L-arginyl-L-lysyl-L-valyl-beta-alanyl-N6-[[1-([2-[(3E)-3-(2,3-dihydro-1H-indolium-1-ylidene)-6-(2,3-dihydro-1H-indol-1-yl)-3H-xanthen-9-yl]phenyl]sulfonyl)piperidin-4-yl]carbonyl]-L-lysyl-N-[(2R)-2-(carboxymethyl)-3-[[(2S)-1-[[(1S)-1,2-dicarboxyethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-3-oxopropyl]-D-phenylalaninamide + L-alanyl-N-[2-[(6-[3,3-dimethyl-2-[(1E,3E,5E)-5-(1,3,3-trimethyl-1,3-dihydro-2H-indol-2-ylidene)penta-1,3-dien-1-yl]-3H-indolium-1-yl]hexanoyl)amino]ethyl]-L-prolinamide
-
Substrates: highly selective substrate for caspase-3
Products: -
Products: -
?
DEVD-NucView488 + H2O
?
-
Substrates: the highly cell-permeable caspase-3 substrate is obtained by linking a fluorogenic DNA-binding dye to the caspase-3 recognition sequence that renders the dye nonfunctional. On substrate cleavage, the dye is released and becomes highly fluorescent on binding to DNA. DEVD-NucView488 detects caspase-3 activation within a live-cell population much earlier and with higher sensitivity compared with other apoptosis reagents. Cells incubated with DEVD-NucView488 exhibit no toxicity and normal apoptotic progression. DEVD-NucView488 is an ideal substrate for kinetic studies of caspase-3 activation because it detects caspase-3 activity in real-time and also efficiently labels DNA in nuclei of caspase-3-activated cells for real-time fluorescent visualization of apoptotic morphology
Products: -
Products: -
?
DNA-dependent protein kinase CS + H2O
?
-
Substrates: cleavage site is DEVD-/-
Products: -
Products: -
?
DW3-FQ + H2O
N2-acetyl-L-lysyl-L-lysyl-L-lysyl-L-arginyl-L-lysyl-L-valyl-beta-alanyl-N6-[[1-([2-[(3E)-3-(2,3-dihydro-1H-indolium-1-ylidene)-6-(2,3-dihydro-1H-indol-1-yl)-3H-xanthen-9-yl]phenyl]sulfonyl)piperidin-4-yl]carbonyl]-L-lysyl-N-[(2R)-2-(carboxymethyl)-3-[[(3S)-1-[[(2S)-1-[[(1S)-1,2-dicarboxyethyl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-5-methyl-1-oxohexan-3-yl]amino]-3-oxopropyl]-D-phenylalaninamide + L-alanyl-N-[2-[(6-[3,3-dimethyl-2-[(1E,3E,5E)-5-(1,3,3-trimethyl-1,3-dihydro-2H-indol-2-ylidene)penta-1,3-dien-1-yl]-3H-indolium-1-yl]hexanoyl)amino]ethyl]-L-prolinamide
-
Substrates: -
Products: -
Products: -
?
glutaredoxin-1 + H2O
?
-
Substrates: murine or human protein substrate, the putative cleavage site of caspase-3, amino acids 56-59 EFVD and 56-59 AIQD, which has predicted affiffinity toward glutamic and aspartic acid residues
Products: cleavage produces a 8 kDA fragment
Products: cleavage produces a 8 kDA fragment
?
IETD-7-amido-4-fluoromethylcoumarin + H2O
IETD + 7-amino-4-fluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
Ile-Glu-Thr-Asp-4-nitroanilide + H2O
Ile-Glu-Thr-Asp + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
LLVY-4-methylcoumarin 7-amide + H2O
LLVY + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
myeloid cell leukemia 1 + H2O
?
-
Substrates: i.e. Mcl-1, apoptosis induced by tumor necrosis factor-related apoptosis-inducing ligand requires specific cleavage of Mcl-1 at D127 and D157 by enzyme. Removal of N-terminal domain of Mcl-1 by enzyme allows for the maximal mitochondrial perturbation that potentiates apoptosis
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Ala-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Ala-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Asn-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Asn-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Glu-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Gly-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Gly-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Pro-Asp-N6-[methyl red]-Lys-6-aminohexanoyl-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: the substrate is able to detect and quantify caspase-3 activity in apoptotic cells without cross-reactivity by caspase-7
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Val-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Val-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
Substrates: -
Products: -
Products: -
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-acetyl-DEVD-4-trifluoromethylcoumarin 7-amide + H2O
N-acetyl-DEVD + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-fluoromethylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-acetyl-DEVD-7-amido-4-methylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-acetyl-DEVD-N'-morpholinecarbonyl-rhodamine 110 + H2O
?
-
Substrates: -
Products: -
Products: -
?
N-acetyl-L-Asp-L-Glu-L-Val-L-Asp-N'-morpholinecarbonyl-rhodamine 110 + H2O
?
-
Substrates: cell-permeable substrate, high turnover rate and sensitivity both in enzyme solution and in living cells
Products: -
Products: -
?
N-acetyl-LDEVD-7-amido-4-methylcoumarin + H2O
N-acetyl-LDEVD + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
N-carbobenzyloxy-DEVD-R110 + H2O
?
-
Substrates: a fluorescent substrate
Products: -
Products: -
?
PAK2 + H2O
?
-
Substrates: caspase-3 is mainly responsible for the apoptotic cleavage of PAK2 in Fas-stimulated Jurkat cells
Products: -
Products: -
?
pro-caspase-6 + H2O
?
-
Substrates: caspase-8 activates caspase-3, and caspase-3 in turn activates caspase-6. Caspase 3 has a major role in nuclear apoptosis
Products: -
Products: -
?
pro-interleukin-18 + H2O
IL18 + ?
-
Substrates: virus infection by influenzy A or Sendai virus induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
Products: -
Products: -
?
RelB + H2O
?
-
Substrates: the Asp205 site in RelB is specifically cleaved by caspase-3 in vinblastine-treated HAT-1080 cells
Products: -
Products: -
?
Rho-GDI 1 + H2O
?
-
Substrates: differential regulation of the homologous GDP dissociation inhibitors Rho-GDI 1 and D4-GDI during drug-induced apoptosis by proteolysis mediated by caspase-3
Products: -
Products: -
?
sterol regulatory element-binding protein + H2O
?
-
Substrates: cleavage site is DEPD-/-
Products: -
Products: -
?
topoisomerase I + H2O
?
-
Substrates: cleavage at DDVD146-/-Y and EEED170-/-G
Products: -
Products: -
?
19 S proteasome + H2O
?
-
Substrates: caspase-3 specifically cleaves the 19 S component of 26 S proteasome Rpt2, Rpt6, and Rpn2 in skeletal muscle stimulating proteasome activity
Products: -
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Ac-DEVD-4-nitroanilide + H2O
Ac-DEVD + 4-nitroaniline
Substrates: an artificial caspase-3 substrate
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Ac-DEVD-4-nitroanilide + H2O
Ac-DEVD + 4-nitroaniline
Substrates: -
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Ac-DEVD-4-nitroanilide + H2O
Ac-DEVD + 4-nitroaniline
Substrates: -
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Ac-DEVD-4-nitroanilide + H2O
Ac-DEVD + 4-nitroaniline
-
Substrates: -
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Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
Substrates: -
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Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
Substrates: the active site of caspase-3 is located at Cys163, which plays a key role in substrate hydration
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acetyl-Asp-Glu-Val-Asp-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Asp-Glu-Val-Asp + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
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acetyl-Asp-Glu-Val-Asp-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Asp-Glu-Val-Asp + 7-amino-4-trifluoromethylcoumarin
-
Substrates: -
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acetyl-Asp-Glu-Val-Asp-p-nitroanilide + H2O
acetyl-Asp-Glu-Val-Asp + p-nitroaniline
-
Substrates: -
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acetyl-Asp-Glu-Val-Asp-p-nitroanilide + H2O
acetyl-Asp-Glu-Val-Asp + p-nitroaniline
-
Substrates: -
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acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
Substrates: high activity
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acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
Substrates: -
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acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
Substrates: -
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acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
Substrates: DEVD is the optimal tetrapeptide recognition motif
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acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
Substrates: -
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acetyl-VDQMDGW-amide + H2O
?
-
Substrates: preferred peptide substrate
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Asp-Glu-Val-Asp-4-nitroanilide + H2O
Asp-Glu-Val-Asp + 4-nitroaniline
-
Substrates: -
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Asp-Glu-Val-Asp-4-nitroanilide + H2O
Asp-Glu-Val-Asp + 4-nitroaniline
-
Substrates: caspase-3 specific substrate
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Asp-Glu-Val-Asp-4-nitroanilide + H2O
Asp-Glu-Val-Asp + 4-nitroaniline
-
Substrates: -
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beta-N-acetylglucosaminidase + H2O
?
-
Substrates: cleavage during apoptosis into two fragments during apoptosis, an N-terminal fragment containing the O-GlcNAcase active site and a C-terminal fragment containing a region with homology to GCN5 histone acetyltransferases, mutation D413A abrogates cleavage by caspase-3 both in vitro and in vivo. O-GlcNAcase activity is not affected by caspase-3 cleavage because the N- and C-terminal O-GlcNAcase fragments remain associated after the cleavage
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beta-N-acetylglucosaminidase + H2O
?
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Substrates: mapping of the celavage site by Edman sequencing, the site is a noncanonical recognition site that occurs after Asp413 of the SVVD sequence in human substrate O-GlcNAcase, mutation D413A abrogates cleavage by caspase-3 both in vitro and in vivo
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cytokeratine 18 + H2O
?
-
Substrates: caspase-induced cytokeratine 18 cleavage in apoptotic cell populations
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DEVD-4-nitroanilide + H2O
DEVD + 4-nitroaniline
Substrates: -
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DEVD-4-nitroanilide + H2O
DEVD + 4-nitroaniline
Substrates: -
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DEVD-4-nitroanilide + H2O
DEVD + 4-nitroaniline
-
Substrates: -
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DEVD-7-amido-4-fluoromethylcoumarin + H2O
DEVD + 7-amino-4-fluoromethylcoumarin
-
Substrates: -
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DEVD-7-amido-4-fluoromethylcoumarin + H2O
DEVD + 7-amino-4-fluoromethylcoumarin
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Substrates: -
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eIF4G + H2O
?
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Substrates: caspase 3 is capable of cleaving eIF4G as part of the translationally active complex eIF4F, thereby inactivating this complex and subsequently causing inhibition of translation in apoptotic cells
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epidermal growth factor receptor + H2O
?
-
Substrates: cleavage during apoptosis
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ICAD + H2O
?
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Substrates: activity of caspase-activated deoxyribonuclease, CAD, is affected by the caspase 3-mediated cleavage of the CAD inhibitor, ICAD
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ICAD + H2O
?
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Substrates: caspase 3-mediated cleavage of the caspase-activated deoxyribonuclease inhibitor, ICAD
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IETD-4-nitroanilide + H2O
IETD + 4-nitroaniline
-
Substrates: -
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mammalian sterile 20-like kinase 1 + H2O
?
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Substrates: i.e. Mst1. Caspase 3 preferentially activates extracellular signal-regulated kinase preferentially through 36000 Da cleaved forms of Mst1. The 36000 Da form of Mst1 selectively phosphorylates extracellular signal-regulated kinase
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mammalian sterile 20-like kinase 1 + H2O
?
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Substrates: i.e. Mst1
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Mcl-1 + H2O
?
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Substrates: antiapoptotic protein. Caspase-3 -mediated Mcl-1 downregulation appears to be responsible for the pro-apoptotic effects of EXEL-0862 on FIP1L1-PDGFRalpha-expressing cells
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MDM2 oncoprotein + H2O
?
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Substrates: because MDM2 functions as a negative regulator of the p53 tumor suppressor and because p53 induces apoptosis in response to a variety of stimuli, this cleavage of MDM2 by CPP32-like proteases may result in deregulation of p53 and contribute directly to the process of apoptotic cell death
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nuclear mitotic apparatus protein + H2O
?
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Substrates: cleavage at sites distinct from caspase-6
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p65/RelA + H2O
?
-
Substrates: caspase-3-mediated carboxy-terminal fragment of p65/RelA production, cells producing this truncated p65/RelA do not undergo apoptosis but show a high viability, in spite of caspase-3 activation, overview. The substrate translocate to the nucleus, associates with NF-kappaB1/p50 and IkappaBalpha, but cannot bind -kappaB consensus sites
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p65/RelA + H2O
?
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Substrates: caspase-3-mediated carboxy-terminal fragment of p65/RelA production, no activity with substrate mutants V91L/D94E, D97E, and D94E/D97E
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poly(ADP-ribose) polymerase + H2O
85000 Da fragment + ?
Substrates: caspase-3 is the predominant poly(ADP-ribose) polymerase cleaving enzyme
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poly(ADP-ribose) polymerase + H2O
85000 Da fragment + ?
Substrates: caspase-3 is the predominant poly(ADP-ribose) polymerase cleaving enzyme
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poly(ADP-ribose) polymerase + H2O
?
-
Substrates: -
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poly(ADP-ribose) polymerase + H2O
?
-
Substrates: caspase cleaves at a DEVD-G motif
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poly(ADP-ribose) polymerase + H2O
?
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Substrates: bovine poly(ADP-ribose) polymerase
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poly(ADP-ribose) polymerase + H2O
?
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Substrates: very high cleavage
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poly(ADP-ribose) polymerase + H2O
?
-
Substrates: cleavage site: DEVD-/-
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pro-Mch2alpha + H2O
?
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Substrates: the enzyme processes pro-Mch2alpha at three aspartate processing sites, Asp23, Asp179, and Asp193, to produce the large p18 and small p11 subunits of the mature Mch2alpha enzyme
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pro-Mch2alpha + H2O
?
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Substrates: the enzyme processes pro-Mch2alpha at three aspartate processing sites, Asp23, Asp179, and Asp193, to produce the large p18 and small p11 subunits of the mature Mch2alpha enzyme. Mch2alpha is a downstream protease activated in CPP32- and granzyme B-mediated apoptosis
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pro-Mch6 + H2O
?
-
Substrates: the enzyme processes proMch6 preferentially at Asp330 to generate two subunits of molecular masses 37000 Da and 10000 Da
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pro-Mch6 + H2O
?
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Substrates: the enzyme processes proMch6 preferentially at Asp330 to generate two subunits of molecular masses 37000 Da and 10000 Da. Mch6 is a downstream protease activated in CPP32- and granzyme B-mediated apoptosis
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procaspase-6 + H2O
caspase-6 + ?
-
Substrates: activation requires caspase-3
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procaspase-6 + H2O
caspase-6 + ?
-
Substrates: activation requires caspase-3
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protein kinase Cdelta + H2O
?
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Substrates: protein kinase Cdelta plays a major role in the regulation of cell apoptosis and survival. PKCdelta is cleaved by caspase 3 to generate a constitutively active catalytic domain that mediates both its apoptotic and anti-apoptotic effects. The phosphorylation of Tyr332 is necessary for the caspase 3-dependent cleavage of protein kinase Cdelta
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protein kinase Cdelta + H2O
?
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Substrates: the phosphorylation of Tyr332 is necessary for the caspase 3-dependent cleavage of protein kinase Cdelta
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protein kinase Czeta + H2O
?
-
Substrates: major cleavage site EETD-/-G, also cleaves at DGMD-/-G and DSED-/-L
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protein kinase Czeta + H2O
?
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Substrates: major cleavage site EETD-/-G, also cleaves at DGMD-/-G and DSED-/-L. Caspase-3 is involved in processing of protein kinase Czeta to carboxyl-terminal fragments that are catalytically active and that are degraded by the ubiquitin-proteasome pathway
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protein phosphatase-1 inhibitor-3 + H2O
?
-
Substrates: the substrate is an in vivo target of caspase-3 and participates in the apoptotic response to induction by actinomycin D, overview
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protein phosphatase-1 inhibitor-3 + H2O
?
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Substrates: recombinant His6-tagged substrate protein expressed in Escherichia coli, substrate mutant D49A is not cleaved by caspase-3
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RFC140 + H2O
?
-
Substrates: cleavage at three sites: DEVD723G, DLVD922S and IETD1117A
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RFC140 + H2O
?
-
Substrates: cleavage of RFC140 during apoptosis inactivates its function in DNA replication and generates truncated forms that further inhibit DNA replication
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Rpt5 + H2O
?
-
Substrates: in myoblasts, Rpt5 is sensitive to caspase-3-induced cleavage but in myotubes, it is not sensitive. Caspase-3 cleavage of Rpt5 is responsible for the difference in the patterns of proteasome subunit cleavage in myoblasts compared with myotubes
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tau protein + H2O
?
Substrates: cleavage by caspase-3 is a crucial upstream event associated with Tau self-assembly leading to Alzheimer's Disease pathogenesis
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tau protein + H2O
?
Substrates: peptides are designed from 441-mer major human Tau protein sequence that encompasses the proposed caspase-3 cleavage site (Asp421-/-Ser422). While the control peptide is efficiently cleaved by caspase-3 at Asp421-/-Ser422 site producing the expected N- and C-terminal fragment peptides, the corresponding phospho-Ser422 peptide remains completely resistant to the cleavage. Substitution of Asp421 by its dextro isoform also blocks peptide cleavage by caspase-3. However substitution of Ser422 by its dextro isoform in the peptide does not affect the cleavage significantly
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transcription factor Pax7 + H2O
?
Substrates: compensatory growth and regeneration of skeletal muscle is dependent on the resident stem cell population, satellite cells (SCs). Self-renewal and maintenance of the SC niche is coordinated by the paired-box transcription factor Pax7. Continued expression of this protein inhibits the myoblast differentiation program. Caspase 3 cleavage inactivation of Pax7 is a crucial step for terminating the self-renewal process
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additional information
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-
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Substrates: apoptosis is a result of a complex network of signaling pathways initiating from both inside and outside the cell, culminating in the activation of caspases, cyteine aspartate proteases, that execute the final stages of cell death
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additional information
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-
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Substrates: characterization of 14 natural zebrafish caspase-3 substrates
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additional information
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-
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Substrates: the preferred cleavage sequence is DEVD-/-
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additional information
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-
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Substrates: the preferred cleavage sequence is DEVD-/-
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additional information
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-
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Substrates: interaction of Hsp27 with the caspase-3 prodomain inhibits the second proteolytic cleavage necessary for caspase-3 activation
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additional information
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-
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Substrates: emodin induces apoptosis through caspase 3-dependent pathway in HK-2 cells
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additional information
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-
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Substrates: caspase-3 is involved in apoptosis
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additional information
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-
-
Substrates: mechanisms of plasma free fatty acid-triggered vascular smooth muscle cell-apoptosis essentially include activation of caspase-3, overview
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additional information
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-
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Substrates: lipopeptide-induced apoptosis in MCF-7 cells is associated with caspase-3
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additional information
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-
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Substrates: caspase-3 is playing a central role in the execution of apoptosis, its activation induces Dox resistance, mechanism, overview
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additional information
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-
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Substrates: the apoptotic effect of cisplatin is caspase-dependent. Caspase-3 inhibitors prevent HA14-1-induced apoptosis in follicular lymphoma B cells
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additional information
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Substrates: caspases are key effectors in the processes of apoptosis and inflammation, executioner caspases selectively hydrolyze cellular proteins in the pathways leading to cell death
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additional information
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-
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Substrates: caspase 3 acts as executioner proteases causing proteolysis of key proteins leading to DNA fragmentation and apoptosis
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additional information
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-
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Substrates: TRAIL and TRAIL death receptors form a complex, which transmits an apoptotic signal via the Fas associated death domain leading to activation of caspase-8 or other initiator caspases, which in turn activate downstream caspases, such as caspase-3, 9, 6 and 7, that cause cell death, overview
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additional information
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-
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Substrates: insulin inhibits caspase-3 activity in renal tubular epithelial cells via the PI3-kinase/Akt pathway
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additional information
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-
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Substrates: constitutive caspase-3 is one of the downstream effectors of TNF-alpha receptor-1 binding, that increases in parallel with the loss of CD28 in long-term T lymphocyte cultures, but this effect is blunted in the presence of the TNF-alpha inhibitors
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additional information
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-
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Substrates: caspase-3 is involved in apoptosis in myeloid leukemia cells, Bcl-2 family proteins are the central regulators of caspases activation, overview
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additional information
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-
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Substrates: human adenovirus type 5 early region 1A, E1A, significantly inhibits the cell proliferation of HeLa by the apoptosis induction through HER-2/Neu/caspase-3 pathway, overview
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additional information
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-
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Substrates: hypertonicity-induced cation channels, HICC, inhibition by flufenamate and silencing of alpha-ENaC increases the rate of apoptosis in HepG2 cells via activation of caspase-3 or caspase-7
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additional information
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-
-
Substrates: caspase-3 is involved in apoptosis
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additional information
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-
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Substrates: caspase-3 is ivolved in apoptosis
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additional information
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-
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Substrates: caspase-3, an effector caspase, is involved in MDA-MB-231 apoptotic cell death, overview. Caspase-3 is activated when procaspase-3 is cleaved subsequently from the recruitment of Fas associated protein with death domain, FADD, to the death-effector domain site of procaspase-8 during the oligomerization of death receptor and its ligand
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additional information
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-
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Substrates: caspase-3 is involved in apoptosis. Follistatin-like 1, FSTL1, induces apoptosis in cancer cells and leads to activation of caspase-3 when transfected to ovarian or endometrial cancer or healthy cells, regulation, overview
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additional information
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-
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Substrates: active caspase-3 is involved in apoptosis in epithelial cells of the intestine
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additional information
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-
-
Substrates: caspase family proteases are key proteins in apoptotic signaling pathways, which are activated in both the death receptor-mediated and the mitochondria-mediated apoptosis pathways
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additional information
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-
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Substrates: caspase-3 has a downstream effector function in apoptosis
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additional information
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-
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Substrates: caspase-3 is an effector caspase. The intrinsic death pathway involves mitochondrial release of cytochrome c, which interacts with Apaf-1 and dATP to promote procaspase-9 autoactivation, which in turn activates downstream effectors such as caspase-3, -6, and -7. Increased caspase-3 activation is involved in apoptosis, inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 and -6 activation, as well as PARP and lamin A/C cleavage and apoptosis, overview. Leptospira interrogans-induced apoptosis in macrophages is mediated by caspase-3 and -6 activation through a FADDcaspase-8-dependent pathway, independently of mitochondrial cytochrome ccaspase-9-dependent signaling. Caspase-3 is required for the activation of caspase-6 and seems to be involved in caspase-9 activation through a feedback amplification loop. Regulation, overview
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additional information
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-
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Substrates: initial activation of caspase-3 causes degradation of glutaredoxin-1, resulting in S-glutathionylation of Fas at cysteine 294, which subsequently enhances binding of FasL, aggregation of Fas, accumulation of Fas in lipid rafts, DISC assembly, and further activation of caspases, causing a propagation of apoptotic cell death. activation of caspases is required for degradation of glutaredoxin-1 and S-glutathionylation of Fas, engagement of Fas causes a rapid activation of caspase-8. Overexpression of Grx1 prevents increases in S-glutathionylation of Fas and attenuates caspase activation and apoptosis in response to receptor ligation. Cleaved caspase-8 and -3 demonstrate an association between active caspases and Grx1 in cells after ligation of Fas, whereas in control cells, these associations are not observed, regulation, overview
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additional information
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Substrates: mycotoxin citrinin has a strong impact on the expression levels of diverse proteins including the caspase-3, citrinin-directed caspase 3 activation involves MAPK signaling pathways, overview
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additional information
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-
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Substrates: homocysteine-mediated EPC toxicity is due to apoptosis involving caspase-8, cytochrome c release, and caspase-3 activation. Vitamin B6, and B9 significantly impair homocysteine-mediated EPC caspase-3 activation in vitro, overview
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additional information
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Substrates: external lactic acid induces apoptosis via the caspase-dependent pathway activating caspase-3, -8, and -9, and the caspase-independent pathway causing increased expressions of AIF and EndoG, overview
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additional information
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-
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Substrates: netrin-1 siRNA-induced H-358 cell death is mediated by caspase-3 and -9 activities, but not by caspase-8 activity
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additional information
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-
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Substrates: caspases 3, 8 and 9 are essential to rhein-induced apoptosis, inhibitors of caspases 3, 8 and 9 are efficiently blocked by rhein-induced apoptosis in TNF-alpha-treated human aortic smooth muscle cells, overview
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additional information
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-
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Substrates: caspase-3 is activated by the death receptor pathway leading to apoptosis. Human herpesvirus HHV-6A-induced apoptosis is associated with activation of caspase-8, caspase-9, and caspase-3, suggesting the involvement of death receptor and mitochondrial signaling pathways, overview. HHV-6 differentially influences the functions of naive T cells and different subsets of memory CD4+ and CD8+ T cells, which in part may be due to differential susceptibility to HHV-6A-induced apoptosis, overview
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additional information
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-
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Substrates: caspase-3 activation results in apoptosis, ischemic/reperfusion in brain leads to increased release of cytochrome c from mitochondria and activation of caspase-3, ischemic preconditioning and ischemic tolerance can diminish the activation of caspase-3, regulation, overview
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additional information
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-
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Substrates: caspase-3, convergent with a variety of death signals, plays a key role in the induction of apoptosis
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additional information
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-
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Substrates: azinomycin epoxide leads to activation and apoptosis in THP-1 cells in a p53-independent manner
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additional information
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-
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Substrates: the extrinsic death receptor pathway of apoptosis proceeding entirely via an intrinsic, Bcl-2-controlled, mitochondrial pathway, does not rely on caspase-9 and requires only limited activation of caspase-3 relative to other chemotherapeutic drugs, overview
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additional information
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-
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Substrates: caspase-3 is an effector caspase
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additional information
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-
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Substrates: the aspartic acid residue in position P1 is a nearly absolute requirement for the caspase activity, at least three additional amino acids at positions P2 to P4 are required to complete the specificity
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additional information
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Substrates: caspase-3 recognizes various P4 residues in its numerous protein substrates, Asp is the most frequent P4 residue in peptide substrates. Although a wide variety of P4 residues in the cellular proteins are cleaved by caspase-3. Hydrophobic residues appear in the relative frequency of Val-Ala-Leu-Met-Phe-Ile/Cys in descending order. The P4 residues forms favorable hydrophobic interactions in two separate hydrophobic regions of the binding site. The side chains of P4 Ile and Tyr form hydrophobic interactions with caspase-3 residues Trp206 and Trp214 within a non-polar pocket of the S4 subsite, while P4 Trp interacts with Phe250 and Phe252 that can also form the S5 subsite, adaptability of caspase-3 for binding diverse P4 residues, substrate specificity, overview
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additional information
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Substrates: caspases contain a reactive cysteine critical for enzymatic activity. Increased S-glutathionylation of Fas, caspase-3 activity, and cell death in cells lacking Grx1
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additional information
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Substrates: caspase-3 cleaves the the DEVD sequence
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additional information
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Substrates: inotodiol, a lanostane triterpenoid, from Inonotus obliquus, inhibits P388 cell proliferation through caspase-3-dependent apoptosis
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additional information
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Substrates: caspase-3 activity is involved in cell death, e.g. induced by simulated ischemia and reperfusion with pH playing an important role, overview
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additional information
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Substrates: caspase-3 is involved in apoptosis
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additional information
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Substrates: caspase-3 is an effector caspase lying downstream from both intrinsic apoptotic pathway mediators and extrinsic apoptotic pathway mediators
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additional information
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Substrates: nonobese diabetic mouse acinar cells at 16 weeks show increased caspase 3 activity, as well as increased expression of TNF-alpha receptor1, increased Bax, tumour protein 53-induced nuclear protein1alpha, and chromatin condensation, apoptosis patterns, overview
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additional information
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Substrates: caspase-3 activity is absent in case of coronary occlusion with and without subsequent revascularization in C57BL6 mice after transient ligation followed by 24 h of reperfusion, or 24 h persistent ligation, overview
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additional information
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Substrates: caspase-3 is an effector caspase. The intrinsic death pathway involves mitochondrial release of cytochrome c, which interacts with Apaf-1 and dATP to promote procaspase-9 autoactivation, which in turn activates downstream effectors such as caspase-3, -6, and -7. Increased caspase-3 activation is involved in apoptosis, inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 and -6 activation, as well as PARP and lamin A/C cleavage and apoptosis, overview. Leptospira interrogans-induced apoptosis in macrophages is mediated by caspase-3 and -6 activation through a FADDcaspase-8-dependent pathway, independently of mitochondrial cytochrome ccaspase-9-dependent signaling. Caspase-3 is required for the activation of caspase-6 and seems to be involved in caspase-9 activation through a feedback amplification loop. Regulation, overview
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additional information
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Substrates: caspase-3 is one of the key executioners of apoptosis and responsible for the partial or total proteolytic cleavage of many proteins. Senescence-accelerated prone mice 8 and senescence-accelerated resistant mice 1 show a drop in age-related proteolytic activity of caspase-3, but the caspase-independent cell death, owing to high p53 and apoptosis-inducing factor levels, might be an alternative pathway of cell death in the aged brain
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additional information
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-
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Substrates: caspases are a family of cysteine aspartic acid-specific proteases playing an important role in apoptotic processes in mammalian cells. Among them, caspase-3 is an essential protease that degrades other protein substrates inside the cells at an early stage of apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: apoptosis is triggered through intrinsic mitochondrial pathway by caspase 3-activation involving mitochondrial membrane potential damage and reactive oxygen species production
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is activated during apoptosis, overexpression of bovine growth hormone has antiapoptotic effects in several cell lines, including human colonic adenocarcinoma cells, and in colonic mucosa reducing the activation of caspase-3, molecular mechanisms and regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 causes chromatin condensation through DNA fragmentation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the caspase-3 cleavage site is present within the ATPase domain of Rpt subunits
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is an effector caspase lying downstream from both intrinsic apoptotic pathway mediators and extrinsic apoptotic pathway mediators
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 activity is absent in case of coronary occlusion with and without subsequent revascularization in C57BL6 mice after transient ligation followed by 24 h of reperfusion, or 24 h persistent ligation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 activity is involved in cell death, e.g. induced by simulated ischemia and reperfusion with pH playing an important role, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: N-methyl-D-aspartate induces the activation of caspase-3 and the caspase-3-dependent apoptotic pathway, the activation is prevented by the autocamtide-2-related inhibitory peptide, overview. Blockade of calcium/calmodulin-dependent protein kinase II-alpha activity prevents N-methyl-D-aspartate-induced caspase-3 activation and provides significant neuroprotection against N-methyl-D-aspartate-induced ganglion cell loss in a retina toxicity model
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme regulation in response to damaging agents like ethanol and acetylsalicylic acid in gastric mucosa, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is involved in glutamate-induced neuronal cell death, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is involved in apoptosis in thymocytes, enzyme inhibition increases cell survival, regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is involved in the ischemic brain injury during experimental stroke. In vitro nitric oxide regulates calpain and caspase-3 activation, and in vivo neuronal nitric oxide synthase, calpain and caspase-3 participate in the ischemic brain injury, inhibition of the neuronal nitric oxide synthase by 7-nitroindazole leads to downregulation of caspase-3, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: activation of caspase-3, an executioner caspase, plays a key role in the apoptotic cascade
Products: -
Products: -
?
additional information
?
-
-
Substrates: increased cytosolic cytochrome c and subsequently caspase-3 activation are additional signs of neuronal death via the mitochondrial pathway. Bradykinin administration significantly attenuates ischemia-induced neuronal death, and also suppresses the release of MnSOD, and cytochrome c, and prevents caspase-3 activation
Products: -
Products: -
?
additional information
?
-
-
Substrates: activated caspase-3 in irradiation-induced microglia death. This age-dependent irradiation-induced loss of microglia likely affects both the response to irradiation and further brain development, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: direct activation of procaspase-3 by caspase-9 and caspase-8 in type I cells, radiation-induced sensitization of hepatocytes to TNF-alpha-mediated apoptosis additionally requires changes upstream of caspase-8 activation, regulation of caspase-8 and apoptosis in hepatocytes, overview. Irradiation induces TNF-alpha-mediated activation of caspase-8, -9, and -3, and apoptosis in hepatocytes. Apoptosis induction is prevented by IkappaB antisense oligonucleotides mediated by suppression of caspases-9 and -3 activation but not of caspase-8 activation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: T-cells show activated caspase-3 with the preservation of photoreceptors
Products: -
Products: -
?
additional information
?
-
-
Substrates: procaspase-3 is activated by caspase-9 and caspase-8
Products: -
Products: -
?
pre-interleukin-1beta + H2O
additional information
-
Substrates: -
Products: a 28000 Da fragement and a 17000 Da fragement, less efficient hydrolysis than with caspase-1
Products: a 28000 Da fragement and a 17000 Da fragement, less efficient hydrolysis than with caspase-1
?
pre-interleukin-1beta + H2O
additional information
-
-
Substrates: -
Products: a 28000 Da fragement and a 17000 Da fragement, less efficient hydrolysis than with caspase-1
Products: a 28000 Da fragement and a 17000 Da fragement, less efficient hydrolysis than with caspase-1
?
pre-interleukin-1beta + H2O
additional information
-
Substrates: -
Products: a 28000 Da fragement and a 17000 Da fragement, less efficient hydrolysis than with caspase-1
Products: a 28000 Da fragement and a 17000 Da fragement, less efficient hydrolysis than with caspase-1
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
19 S proteasome + H2O
?
-
Substrates: caspase-3 specifically cleaves the 19 S component of 26 S proteasome Rpt2, Rpt6, and Rpn2 in skeletal muscle stimulating proteasome activity
Products: -
Products: -
?
anamorsin + H2O
?
-
Substrates: specifically cleaved by caspase-3 at DSVD209 L generating 25- and 10-kDa fragments
Products: -
Products: -
?
beta-catenin + H2O
?
-
Substrates: processing of beta-catenin, production of a 70000 Da fragment
Products: -
Products: -
?
beta-N-acetylglucosaminidase + H2O
?
-
Substrates: cleavage during apoptosis into two fragments during apoptosis, an N-terminal fragment containing the O-GlcNAcase active site and a C-terminal fragment containing a region with homology to GCN5 histone acetyltransferases, mutation D413A abrogates cleavage by caspase-3 both in vitro and in vivo. O-GlcNAcase activity is not affected by caspase-3 cleavage because the N- and C-terminal O-GlcNAcase fragments remain associated after the cleavage
Products: -
Products: -
?
caspase 9 + H2O
?
-
Substrates: cleavage by caspase 3 does not result in activation of caspase 9, but enhances apoptosis by alleviating XIAP inhibition of the apical caspase
Products: -
Products: -
?
cytokeratine 18 + H2O
?
-
Substrates: caspase-induced cytokeratine 18 cleavage in apoptotic cell populations
Products: -
Products: -
?
D4-GDI(Rho-GDI 2) + H2O
?
-
Substrates: differential regulation of the homologous GDP dissociation inhibitors Rho-GDI 1 and D4-GDI during drug-induced apoptosis by proteolysis mediated by caspase-3
Products: -
Products: -
?
eIF4G + H2O
?
-
Substrates: caspase 3 is capable of cleaving eIF4G as part of the translationally active complex eIF4F, thereby inactivating this complex and subsequently causing inhibition of translation in apoptotic cells
Products: -
Products: -
?
epidermal growth factor receptor + H2O
?
-
Substrates: cleavage during apoptosis
Products: -
Products: -
?
ICAD + H2O
?
-
Substrates: activity of caspase-activated deoxyribonuclease, CAD, is affected by the caspase 3-mediated cleavage of the CAD inhibitor, ICAD
Products: -
Products: -
?
mammalian sterile 20-like kinase 1 + H2O
?
-
Substrates: i.e. Mst1. Caspase 3 preferentially activates extracellular signal-regulated kinase preferentially through 36000 Da cleaved forms of Mst1. The 36000 Da form of Mst1 selectively phosphorylates extracellular signal-regulated kinase
Products: -
Products: -
?
Mcl-1 + H2O
?
-
Substrates: antiapoptotic protein. Caspase-3 -mediated Mcl-1 downregulation appears to be responsible for the pro-apoptotic effects of EXEL-0862 on FIP1L1-PDGFRalpha-expressing cells
Products: -
Products: -
?
MDM2 oncoprotein + H2O
?
-
Substrates: because MDM2 functions as a negative regulator of the p53 tumor suppressor and because p53 induces apoptosis in response to a variety of stimuli, this cleavage of MDM2 by CPP32-like proteases may result in deregulation of p53 and contribute directly to the process of apoptotic cell death
Products: -
Products: -
?
myeloid cell leukemia 1 + H2O
?
-
Substrates: i.e. Mcl-1, apoptosis induced by tumor necrosis factor-related apoptosis-inducing ligand requires specific cleavage of Mcl-1 at D127 and D157 by enzyme. Removal of N-terminal domain of Mcl-1 by enzyme allows for the maximal mitochondrial perturbation that potentiates apoptosis
Products: -
Products: -
?
N-acetyl-DEVD-7-amido-4-methylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
p65/RelA + H2O
?
-
Substrates: caspase-3-mediated carboxy-terminal fragment of p65/RelA production, cells producing this truncated p65/RelA do not undergo apoptosis but show a high viability, in spite of caspase-3 activation, overview. The substrate translocate to the nucleus, associates with NF-kappaB1/p50 and IkappaBalpha, but cannot bind -kappaB consensus sites
Products: -
Products: -
?
PAK2 + H2O
?
-
Substrates: caspase-3 is mainly responsible for the apoptotic cleavage of PAK2 in Fas-stimulated Jurkat cells
Products: -
Products: -
?
pro-caspase-6 + H2O
?
-
Substrates: caspase-8 activates caspase-3, and caspase-3 in turn activates caspase-6. Caspase 3 has a major role in nuclear apoptosis
Products: -
Products: -
?
pro-interleukin-18 + H2O
IL18 + ?
-
Substrates: virus infection by influenzy A or Sendai virus induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
Products: -
Products: -
?
pro-Mch2alpha + H2O
?
-
Substrates: the enzyme processes pro-Mch2alpha at three aspartate processing sites, Asp23, Asp179, and Asp193, to produce the large p18 and small p11 subunits of the mature Mch2alpha enzyme. Mch2alpha is a downstream protease activated in CPP32- and granzyme B-mediated apoptosis
Products: -
Products: -
?
pro-Mch6 + H2O
?
-
Substrates: the enzyme processes proMch6 preferentially at Asp330 to generate two subunits of molecular masses 37000 Da and 10000 Da. Mch6 is a downstream protease activated in CPP32- and granzyme B-mediated apoptosis
Products: -
Products: -
?
protein kinase Cdelta + H2O
?
-
Substrates: protein kinase Cdelta plays a major role in the regulation of cell apoptosis and survival. PKCdelta is cleaved by caspase 3 to generate a constitutively active catalytic domain that mediates both its apoptotic and anti-apoptotic effects. The phosphorylation of Tyr332 is necessary for the caspase 3-dependent cleavage of protein kinase Cdelta
Products: -
Products: -
?
protein kinase Czeta + H2O
?
-
Substrates: major cleavage site EETD-/-G, also cleaves at DGMD-/-G and DSED-/-L. Caspase-3 is involved in processing of protein kinase Czeta to carboxyl-terminal fragments that are catalytically active and that are degraded by the ubiquitin-proteasome pathway
Products: -
Products: -
?
protein phosphatase-1 inhibitor-3 + H2O
?
-
Substrates: the substrate is an in vivo target of caspase-3 and participates in the apoptotic response to induction by actinomycin D, overview
Products: -
Products: -
?
RelB + H2O
?
-
Substrates: the Asp205 site in RelB is specifically cleaved by caspase-3 in vinblastine-treated HAT-1080 cells
Products: -
Products: -
?
RFC140 + H2O
?
-
Substrates: cleavage of RFC140 during apoptosis inactivates its function in DNA replication and generates truncated forms that further inhibit DNA replication
Products: -
Products: -
?
Rho-GDI 1 + H2O
?
-
Substrates: differential regulation of the homologous GDP dissociation inhibitors Rho-GDI 1 and D4-GDI during drug-induced apoptosis by proteolysis mediated by caspase-3
Products: -
Products: -
?
Rpt5 + H2O
?
-
Substrates: in myoblasts, Rpt5 is sensitive to caspase-3-induced cleavage but in myotubes, it is not sensitive. Caspase-3 cleavage of Rpt5 is responsible for the difference in the patterns of proteasome subunit cleavage in myoblasts compared with myotubes
Products: -
Products: -
?
tau protein + H2O
?
Substrates: cleavage by caspase-3 is a crucial upstream event associated with Tau self-assembly leading to Alzheimer's Disease pathogenesis
Products: -
Products: -
?
topoisomerase I + H2O
?
-
Substrates: cleavage at DDVD146-/-Y and EEED170-/-G
Products: -
Products: -
?
transcription factor Pax7 + H2O
?
Substrates: compensatory growth and regeneration of skeletal muscle is dependent on the resident stem cell population, satellite cells (SCs). Self-renewal and maintenance of the SC niche is coordinated by the paired-box transcription factor Pax7. Continued expression of this protein inhibits the myoblast differentiation program. Caspase 3 cleavage inactivation of Pax7 is a crucial step for terminating the self-renewal process
Products: -
Products: -
?
poly(ADP-ribose) polymerase + H2O
85000 Da fragment + ?
Substrates: caspase-3 is the predominant poly(ADP-ribose) polymerase cleaving enzyme
Products: -
Products: -
?
poly(ADP-ribose) polymerase + H2O
85000 Da fragment + ?
Substrates: caspase-3 is the predominant poly(ADP-ribose) polymerase cleaving enzyme
Products: -
Products: -
?
procaspase-6 + H2O
caspase-6 + ?
-
Substrates: activation requires caspase-3
Products: -
Products: -
?
procaspase-6 + H2O
caspase-6 + ?
-
Substrates: activation requires caspase-3
Products: -
Products: -
?
additional information
?
-
-
Substrates: apoptosis is a result of a complex network of signaling pathways initiating from both inside and outside the cell, culminating in the activation of caspases, cyteine aspartate proteases, that execute the final stages of cell death
Products: -
Products: -
?
additional information
?
-
-
Substrates: characterization of 14 natural zebrafish caspase-3 substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction of Hsp27 with the caspase-3 prodomain inhibits the second proteolytic cleavage necessary for caspase-3 activation
Products: -
Products: -
?
additional information
?
-
-
Substrates: emodin induces apoptosis through caspase 3-dependent pathway in HK-2 cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is involved in apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: mechanisms of plasma free fatty acid-triggered vascular smooth muscle cell-apoptosis essentially include activation of caspase-3, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: lipopeptide-induced apoptosis in MCF-7 cells is associated with caspase-3
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is playing a central role in the execution of apoptosis, its activation induces Dox resistance, mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the apoptotic effect of cisplatin is caspase-dependent. Caspase-3 inhibitors prevent HA14-1-induced apoptosis in follicular lymphoma B cells
Products: -
Products: -
?
additional information
?
-
Substrates: caspases are key effectors in the processes of apoptosis and inflammation, executioner caspases selectively hydrolyze cellular proteins in the pathways leading to cell death
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase 3 acts as executioner proteases causing proteolysis of key proteins leading to DNA fragmentation and apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: TRAIL and TRAIL death receptors form a complex, which transmits an apoptotic signal via the Fas associated death domain leading to activation of caspase-8 or other initiator caspases, which in turn activate downstream caspases, such as caspase-3, 9, 6 and 7, that cause cell death, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: insulin inhibits caspase-3 activity in renal tubular epithelial cells via the PI3-kinase/Akt pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: constitutive caspase-3 is one of the downstream effectors of TNF-alpha receptor-1 binding, that increases in parallel with the loss of CD28 in long-term T lymphocyte cultures, but this effect is blunted in the presence of the TNF-alpha inhibitors
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is involved in apoptosis in myeloid leukemia cells, Bcl-2 family proteins are the central regulators of caspases activation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: human adenovirus type 5 early region 1A, E1A, significantly inhibits the cell proliferation of HeLa by the apoptosis induction through HER-2/Neu/caspase-3 pathway, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: hypertonicity-induced cation channels, HICC, inhibition by flufenamate and silencing of alpha-ENaC increases the rate of apoptosis in HepG2 cells via activation of caspase-3 or caspase-7
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is involved in apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is ivolved in apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3, an effector caspase, is involved in MDA-MB-231 apoptotic cell death, overview. Caspase-3 is activated when procaspase-3 is cleaved subsequently from the recruitment of Fas associated protein with death domain, FADD, to the death-effector domain site of procaspase-8 during the oligomerization of death receptor and its ligand
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is involved in apoptosis. Follistatin-like 1, FSTL1, induces apoptosis in cancer cells and leads to activation of caspase-3 when transfected to ovarian or endometrial cancer or healthy cells, regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: active caspase-3 is involved in apoptosis in epithelial cells of the intestine
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase family proteases are key proteins in apoptotic signaling pathways, which are activated in both the death receptor-mediated and the mitochondria-mediated apoptosis pathways
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 has a downstream effector function in apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is an effector caspase. The intrinsic death pathway involves mitochondrial release of cytochrome c, which interacts with Apaf-1 and dATP to promote procaspase-9 autoactivation, which in turn activates downstream effectors such as caspase-3, -6, and -7. Increased caspase-3 activation is involved in apoptosis, inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 and -6 activation, as well as PARP and lamin A/C cleavage and apoptosis, overview. Leptospira interrogans-induced apoptosis in macrophages is mediated by caspase-3 and -6 activation through a FADDcaspase-8-dependent pathway, independently of mitochondrial cytochrome ccaspase-9-dependent signaling. Caspase-3 is required for the activation of caspase-6 and seems to be involved in caspase-9 activation through a feedback amplification loop. Regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: initial activation of caspase-3 causes degradation of glutaredoxin-1, resulting in S-glutathionylation of Fas at cysteine 294, which subsequently enhances binding of FasL, aggregation of Fas, accumulation of Fas in lipid rafts, DISC assembly, and further activation of caspases, causing a propagation of apoptotic cell death. activation of caspases is required for degradation of glutaredoxin-1 and S-glutathionylation of Fas, engagement of Fas causes a rapid activation of caspase-8. Overexpression of Grx1 prevents increases in S-glutathionylation of Fas and attenuates caspase activation and apoptosis in response to receptor ligation. Cleaved caspase-8 and -3 demonstrate an association between active caspases and Grx1 in cells after ligation of Fas, whereas in control cells, these associations are not observed, regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: mycotoxin citrinin has a strong impact on the expression levels of diverse proteins including the caspase-3, citrinin-directed caspase 3 activation involves MAPK signaling pathways, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: homocysteine-mediated EPC toxicity is due to apoptosis involving caspase-8, cytochrome c release, and caspase-3 activation. Vitamin B6, and B9 significantly impair homocysteine-mediated EPC caspase-3 activation in vitro, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: external lactic acid induces apoptosis via the caspase-dependent pathway activating caspase-3, -8, and -9, and the caspase-independent pathway causing increased expressions of AIF and EndoG, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: netrin-1 siRNA-induced H-358 cell death is mediated by caspase-3 and -9 activities, but not by caspase-8 activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspases 3, 8 and 9 are essential to rhein-induced apoptosis, inhibitors of caspases 3, 8 and 9 are efficiently blocked by rhein-induced apoptosis in TNF-alpha-treated human aortic smooth muscle cells, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is activated by the death receptor pathway leading to apoptosis. Human herpesvirus HHV-6A-induced apoptosis is associated with activation of caspase-8, caspase-9, and caspase-3, suggesting the involvement of death receptor and mitochondrial signaling pathways, overview. HHV-6 differentially influences the functions of naive T cells and different subsets of memory CD4+ and CD8+ T cells, which in part may be due to differential susceptibility to HHV-6A-induced apoptosis, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 activation results in apoptosis, ischemic/reperfusion in brain leads to increased release of cytochrome c from mitochondria and activation of caspase-3, ischemic preconditioning and ischemic tolerance can diminish the activation of caspase-3, regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3, convergent with a variety of death signals, plays a key role in the induction of apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: azinomycin epoxide leads to activation and apoptosis in THP-1 cells in a p53-independent manner
Products: -
Products: -
?
additional information
?
-
-
Substrates: the extrinsic death receptor pathway of apoptosis proceeding entirely via an intrinsic, Bcl-2-controlled, mitochondrial pathway, does not rely on caspase-9 and requires only limited activation of caspase-3 relative to other chemotherapeutic drugs, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: inotodiol, a lanostane triterpenoid, from Inonotus obliquus, inhibits P388 cell proliferation through caspase-3-dependent apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 activity is involved in cell death, e.g. induced by simulated ischemia and reperfusion with pH playing an important role, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is involved in apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is an effector caspase lying downstream from both intrinsic apoptotic pathway mediators and extrinsic apoptotic pathway mediators
Products: -
Products: -
?
additional information
?
-
-
Substrates: nonobese diabetic mouse acinar cells at 16 weeks show increased caspase 3 activity, as well as increased expression of TNF-alpha receptor1, increased Bax, tumour protein 53-induced nuclear protein1alpha, and chromatin condensation, apoptosis patterns, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 activity is absent in case of coronary occlusion with and without subsequent revascularization in C57BL6 mice after transient ligation followed by 24 h of reperfusion, or 24 h persistent ligation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is an effector caspase. The intrinsic death pathway involves mitochondrial release of cytochrome c, which interacts with Apaf-1 and dATP to promote procaspase-9 autoactivation, which in turn activates downstream effectors such as caspase-3, -6, and -7. Increased caspase-3 activation is involved in apoptosis, inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 and -6 activation, as well as PARP and lamin A/C cleavage and apoptosis, overview. Leptospira interrogans-induced apoptosis in macrophages is mediated by caspase-3 and -6 activation through a FADDcaspase-8-dependent pathway, independently of mitochondrial cytochrome ccaspase-9-dependent signaling. Caspase-3 is required for the activation of caspase-6 and seems to be involved in caspase-9 activation through a feedback amplification loop. Regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is one of the key executioners of apoptosis and responsible for the partial or total proteolytic cleavage of many proteins. Senescence-accelerated prone mice 8 and senescence-accelerated resistant mice 1 show a drop in age-related proteolytic activity of caspase-3, but the caspase-independent cell death, owing to high p53 and apoptosis-inducing factor levels, might be an alternative pathway of cell death in the aged brain
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspases are a family of cysteine aspartic acid-specific proteases playing an important role in apoptotic processes in mammalian cells. Among them, caspase-3 is an essential protease that degrades other protein substrates inside the cells at an early stage of apoptosis
Products: -
Products: -
?
additional information
?
-
-
Substrates: apoptosis is triggered through intrinsic mitochondrial pathway by caspase 3-activation involving mitochondrial membrane potential damage and reactive oxygen species production
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is activated during apoptosis, overexpression of bovine growth hormone has antiapoptotic effects in several cell lines, including human colonic adenocarcinoma cells, and in colonic mucosa reducing the activation of caspase-3, molecular mechanisms and regulation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 is an effector caspase lying downstream from both intrinsic apoptotic pathway mediators and extrinsic apoptotic pathway mediators
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 activity is absent in case of coronary occlusion with and without subsequent revascularization in C57BL6 mice after transient ligation followed by 24 h of reperfusion, or 24 h persistent ligation, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: caspase-3 activity is involved in cell death, e.g. induced by simulated ischemia and reperfusion with pH playing an important role, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: N-methyl-D-aspartate induces the activation of caspase-3 and the caspase-3-dependent apoptotic pathway, the activation is prevented by the autocamtide-2-related inhibitory peptide, overview. Blockade of calcium/calmodulin-dependent protein kinase II-alpha activity prevents N-methyl-D-aspartate-induced caspase-3 activation and provides significant neuroprotection against N-methyl-D-aspartate-induced ganglion cell loss in a retina toxicity model
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme regulation in response to damaging agents like ethanol and acetylsalicylic acid in gastric mucosa, overview
Products: -
Products: -
?
additional information
?
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Substrates: caspase-3 is involved in glutamate-induced neuronal cell death, overview
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Substrates: caspase-3 is involved in apoptosis in thymocytes, enzyme inhibition increases cell survival, regulation, overview
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Substrates: caspase-3 is involved in the ischemic brain injury during experimental stroke. In vitro nitric oxide regulates calpain and caspase-3 activation, and in vivo neuronal nitric oxide synthase, calpain and caspase-3 participate in the ischemic brain injury, inhibition of the neuronal nitric oxide synthase by 7-nitroindazole leads to downregulation of caspase-3, mechanism, overview
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Substrates: activation of caspase-3, an executioner caspase, plays a key role in the apoptotic cascade
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Substrates: increased cytosolic cytochrome c and subsequently caspase-3 activation are additional signs of neuronal death via the mitochondrial pathway. Bradykinin administration significantly attenuates ischemia-induced neuronal death, and also suppresses the release of MnSOD, and cytochrome c, and prevents caspase-3 activation
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Substrates: activated caspase-3 in irradiation-induced microglia death. This age-dependent irradiation-induced loss of microglia likely affects both the response to irradiation and further brain development, overview
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Substrates: direct activation of procaspase-3 by caspase-9 and caspase-8 in type I cells, radiation-induced sensitization of hepatocytes to TNF-alpha-mediated apoptosis additionally requires changes upstream of caspase-8 activation, regulation of caspase-8 and apoptosis in hepatocytes, overview. Irradiation induces TNF-alpha-mediated activation of caspase-8, -9, and -3, and apoptosis in hepatocytes. Apoptosis induction is prevented by IkappaB antisense oligonucleotides mediated by suppression of caspases-9 and -3 activation but not of caspase-8 activation, overview
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Substrates: T-cells show activated caspase-3 with the preservation of photoreceptors
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3R)-3-ethyl-1-[methyl(octyl)amino]-6-[3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]octane-2,5-dione
-
50% inhibition at 9 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-3-ethyl-6-[2-oxo-3-[(1,3-thiazol-5-ylmethyl)amino]pyrazin-1(2H)-yl]-1-(phenylsulfanyl)octane-2,5-dione
-
50% inhibition at 12 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-3-ethyl-6-[3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-1-(phenylsulfanyl)octane-2,5-dione
-
50% inhibition at 7.9 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-3-ethyl-6-[5-ethyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-1-[hexyl(methyl)amino]octane-2,5-dione
-
50% inhibition at 6 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-6-[5-tert-butyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-3-ethyl-1-[hexyl(methyl)amino]octane-2,5-dione
-
i.e. M826, 50% inhibition at 6 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-6-[5-tert-butyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-3-ethyl-1-[methyl(pentyl)amino]octane-2,5-dione
-
i.e. M867, 50% inhibition at 0.1 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(2-phenylethyl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(pyridin-3-yl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-[2-[(thiophen-2-ylacetyl)amino]ethyl]-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-8-(2-[[(4-chlorophenyl)acetyl]amino]ethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-[2-[(1H-benzimidazol-6-ylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-[2-[(cyclohexylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-[(2-[3-[(N-acetyl-L-alpha-aspartyl)amino]-2-oxopyridin-1(2H)-yl]butanoyl)amino]-5-(benzylsulfanyl)-4-oxopentanoic acid
-
50% inhibition at 52 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-3-[(2-[3-[(N-acetyl-L-alpha-aspartyl)amino]-2-oxopyridin-1(2H)-yl]butanoyl)amino]-5-[(2-chloro-6-fluorobenzyl)sulfanyl]-4-oxopentanoic acid
-
50% inhibition at 0.3 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-3-[[(2-[4-carboxy-2-[(phenylacetyl)amino]butyl]-1,3-dioxo-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl)carbonyl]amino]-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-[[(2R)-2-[3-[(naphthalen-2-ylcarbonyl)amino]-2-oxopyridin-1(2H)-yl]-2-phenylacetyl]amino]-4-oxo-5-phenoxypentanoic acid
-
-
(3S)-5-(2,6-difluorophenoxy)-3-([[(2-methoxyphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-(2,6-difluorophenoxy)-3-([[(3-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-(2,6-difluorophenoxy)-3-([[(4-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-(benzylsulfanyl)-3-([N-[(2,5-dimethoxyphenyl)acetyl]-L-valyl]amino)-4-oxopentanoic acid
-
50% inhibition at 48 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-5-(benzylsulfanyl)-3-[(N-[[2-ethoxy-5-(2-methoxy-2-oxoethoxy)phenyl]acetyl]-L-valyl)amino]-4-oxopentanoic acid
-
50% inhibition at 86 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-5-fluoro-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-[(2,6-dichlorobenzoyl)oxy]-3-[([1,3-dioxo-2-[2-(1H-tetrazol-5-yl)ethyl]-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl]carbonyl)amino]-4-oxopentanoic acid
-
-
(3S)-5-[(2-chloro-6-fluorobenzyl)sulfanyl]-3-[(N-[[2-ethoxy-5-(2-methoxy-2-oxoethoxy)phenyl]acetyl]-L-valyl)amino]-4-oxopentanoic acid
-
50% inhibition at 53 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(4S,7S,10S,13S)-7-(2-carboxyethyl)-4-(carboxymethyl)-13-(cyclobutylcarbonyl)-10-(1-methylethyl)-2,5,8,11-tetraoxo-3,6,9,12-tetraazapentadecan-15-oic acid
-
non-preferred name, comparison with inhibition of caspase-7
(S)-(+)-5-[1-[2-(thiophenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 44 nM
(S)-1-((1-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-1H-1,2,3-triazol-4-yl)methyl)-5-((2-(methoxymethyl)pyrrolidin-1-yl)sulfonyl)indoline-2,3-dione
-
-
(S)-1-(11,11-difluoroundecyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-chloro-2-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(4-pyridinylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
IC50: 4.2 nM
(S)-1-(carboxymethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 170 nM
(S)-1-(cyclohexylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
IC50: 5.2 nM
(S)-1-allyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 4.6 nM
(S)-1-benzyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 2.5 nM
(S)-1-methyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 30 nM
(S)-1-[(tert-butyloxycarbonyl)methyl]-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 3.1 nM
(S)-1-[3-(3-fluoropropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-[3-(3-hydroxypropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-[3-[3-(2-fluoroethoxy)propoxy]propyl]-5-[1-(2-methoxymethylpyrrolidinyl)-sulfonyl]isatin
-
-
(S)-3,3-difluoro-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
-
-
(S)-3,3-difluoro-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
-
-
(S)-3,5-bis-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-3-[3-[5-(1-(2-methoxymethylpyrrolidinyl)sulfonyl)-2,3-dioxoindolin-1-yl]propoxy]-propyl methanesulfonate
-
-
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propanoic acid
-
-
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propyl methanesulfonate
-
-
(S)-3-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-pyridin-2-ylmethyl]sulfamoyl]benzoic acid
-
-
(S)-3-[[6-(benzenesulfonylamino-methyl)pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-acetylsulfamoyl-benzenesulfonylamino)-methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-methanesulfonyl-benzenesulfonylamino)-methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-methanesulfonylamino-benzenesulfonylamino)methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-methanesulfonylaminocarbonyl-benzenesulfonylamino)methyl]-pyridine-3-carbonyl]amino]-4-oxobutyric acid
-
-
(S)-3-[[6-[(4-hydroxy-benzenesulfonylamino)methyl]-pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(4-methanesulfonylamino-benzenesulfonylamino)methyl]pyridien-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-4-oxo-3-[[6-[[3-(1H-tetrazol-5-yl)benzenesulfonylamino]methyl]pyridine-3-carbonyl]amino]butyric acid
-
-
(S)-4-oxo-3-[[6-[[3-(5-oxo-4,5-dihydro[1,2,4]oxadiazol-3-yl)benzenesulfonylamino]methyl]pyridien-3-carbonyl]amino]butyric acid
-
-
(S)-4-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-4-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]butyl 4-methyl-benzenesulfonate
-
-
(S)-4-[[4-(hydroxy-3-methyl-benzenesulfonylamino)methyl]thiophene]-2-carboxylic acid [3-(2-chloro-benzylsulfanyl)-1-ethyl-2-oxo-propyl]amide
-
-
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,3,3-trifluoropropyl)isatin
-
-
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,4,4-trifluorobut-3-enyl)isatin
-
-
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(4,4,4-trifluorobutyl)isatin
-
-
(S)-5-[1-[(2-tert-butoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
IC50: 70 nM
(S)-5-[1-[2-(phenylaminocarbonyl)pyrrolidinyl]sulfonyl]isatin
IC50: 140 nM
(S)-5-[1-[[2-(dimethylamino)carbonyl]pyrrolidinyl]sulfonyl]isatin
IC50: 410 nM
(S)-5-[[3-(1-carboxymethyl-2-oxo-ethylcarbamoyl)isooxazol-5-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[3-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]isoxazol-5-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[4-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-4-methyl-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-furan-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-pyrazin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiazol-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-3-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyrimidin-2-ylmethyl]sulfamoyl]-2-hydroxybenzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-3-methylsulfanyl-2-oxo-propylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-2-oxo-3-(pyridin-3-ylmethylsulfanyl)propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-2-oxo-3-(pyridin-4-ylmethylsulfanyl)propylcarbamoyl]thiophen-2-ylmethyl]-sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]-4-methyl-thiophen-2-ylmethyl]-sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]furan-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyrazin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyrimidin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiazol-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-3-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-5-(2-chloro-phenyl)-2-oxopentylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
1-methyl-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-methyl-5-[[(3R)-3-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
i.e. GSK-31, inhibitory effect is greatest in presence of 2-mercaptoethanol and decreases 2fold by substitution of 2-mercaptoethanol with dithiothreitol
1-[[1-(2,3-dihydro-1,4-benzodioxin-6-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
2,4-dimethyl-8-(morpholin-4-ylsulfonyl)-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
50% inhibition at 0.000044 mM
2-(2,6-dihydroxyphenyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-(2-hydroxyethyl)-4-methyl-8-[(4-methylpiperidin-1-yl)sulfonyl]-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
i.e. CD-001-0011, 50% inhibition at 130 nM, reversible, inhibitory effect is greatest in presence of dithiothreitol and decreases 3-4fold by substitution of dithiothreitol with 2-mercaptoethanol
2-(chloroacetyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-amino-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-chloro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)acetamide
-
50% inhibition at 92 nM
2-methoxy-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)benzamide
-
50% inhibition at 96 nM
2-methoxy-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)benzamide
-
50% inhibition at 103 nM
2-nitro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)benzamide
-
50% inhibition at 62 nM
2-[(2,6-dihydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(2-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(3,5-diamino-4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[3-(4-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
most potent inhibitor
3,3-dimethyl-8-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-3,4-dihydropyrimido[1,2-a]indol-10(2H)-one
-
-
3-({2-[5-tert-butyl-3-{[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino}-2-oxopyrazin-1(2H)-yl]butanoyl}amino)-5-[methyl(pentyl)amino]-4-oxopentanoic acid
3-chloro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)propanamide
-
50% inhibition at 83 nM, comparison with inhibitory effect on caspase-2, caspase-6, caspase-7, caspase-8, papain, proteasome, trypsin and thrombin
3-hydroxyl-anthranilamide
-
inhibits caspase-3, the compound is isolated from Streptomyces sp., a mangrove actinomycete, strain 061316
3-nitro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)benzamide
-
50% inhibition at 53 nM
3-oxo-N-[4-(piperidin-1-ylsulfonyl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
-
-
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
-
-
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-5-(2,6-difluorophenoxy)-4-oxopentanoic acid
-
-
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
-
-
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-5-(2,6-difluorophenoxy)-4-oxopentanoic acid
-
-
3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
-
-
3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
-
-
4-(ethoxycarbonylmethoxy)-1-hydroxy-2-naphthoic acid
-
CS4566, a caspase-3-specific small molecular inhibitor, binding mode, overview
4-fluoro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)benzamide
-
50% inhibition at 99 nM
4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-carbonitrile
-
50% inhibition at 0.000016 mM
4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonamide
-
50% inhibition at 0.000033 mM
4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonic acid
-
50% inhibition at 0.00009 mM
4-methyl-2-(1-methylethyl)-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
4-methyl-8-(morpholin-4-ylsulfonyl)-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
50% inhibition at 0.00021 mM
4-methyl-8-(morpholin-4-ylsulfonyl)-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
50% inhibition at 0.000004 mM
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(1,3-thiazol-2-yl)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(2,4,6-trihydroxyphenyl)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(phenylamino)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-[(2,4,6-trihydroxyphenyl)amino]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
4-methyl-8-[[(2R)-2-phenoxypyrrolidin-1-yl]sulfonyl]-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
50% inhibition at 0.000055 mM
4-nitro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)benzamide
-
50% inhibition at 54 nM
4-oxo-4-piperidin-1-yl-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)butanamide
-
50% inhibition at 25 nM, comparison with inhibitory effect on caspase-2, caspase-6, caspase-7, caspase-8, papain, proteasome, trypsin and thrombin
4-oxo-4-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)amino]butanoic acid
-
50% inhibition at 68 nM, comparison with inhibitory effect on caspase-2, caspase-6, caspase-7, caspase-8, papain, proteasome, trypsin and thrombin
4-[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl]benzoic acid
-
-
4-[5-([(3S)-1-[(2,6-dichlorobenzoyl)oxy]-2,5-dioxohexan-3-yl]carbamoyl)-1,3-dioxo-8-(thiophen-2-yl)-5,8-dihydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-2(3H)-yl]butanoic acid
-
-
5-(2,6-difluorophenoxy)-3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
-
-
5-(2,6-difluorophenoxy)-3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
-
-
5-(2,6-difluorophenoxy)-3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
-
-
5-([(2R)-2-[(2,4-difluorophenoxy)methyl]pyrrolidin-1-yl]sulfonyl)-1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
-
-
5-([(2S)-2-[(pyridin-3-yloxy)methyl]pyrrolidin-1-yl]sulfonyl)-1H-indole-2,3-dione
-
-
5-oxo-5-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)amino]pentanoic acid
-
50% inhibition at 79 nM
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-4-yl]methyl)-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-5-yl]methyl)-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-4-yl)ethyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-5-yl)ethyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-phenyl-1H-indole-2,3-dione
-
-
5-[[5-[1-carboxymethyl-2-(7-methyl-benzoxazol-2-yl)-2-oxo-ethylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
5-[[5-[1-carboxymethyl-2-[5-(2,6-dichloro-phenyl)-oxazol-2-yl]-2-oxo-ethylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
8-hydroxyl-2,4-dioxoquinazoline
-
inhibits caspase-3, the compound is isolated from Streptomyces sp., a mangrove actinomycete, strain 061316
8-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-3,3-dimethyl-3,4-dihydropyrimido[1,2-a]indol-10(2H)-one
-
-
Ac-ADRTD-CHO
moderate inhibitory affinity for caspase-2 with approximately the same affinity for caspase-3
-
Ac-Asp-Glu-Val-Asp-H
-
the molecule can be truncated to Z-tLeu-Asp-H retaining nanomolar inhibitory activity in vitro and displaying action in whole cells, overview
Ac-DNLD-CHO
-
from rational computational design, the inhibitor is specific due to the specific interaction of the NLD moiety with the active site of caspase-3, docking mode and site-directed mutagenesis analysis. In the active site of caspase-3, Asn in Ac-DNLDCHO specifically interacts with Ser209 in the S3 subsite, and Leu tightly interacts with the hydrophobic S2 subsite, overview
Ac-FDVPD-CHO
pKi: 8.15/8.03. Little selectivity for caspase-2 over caspase-3
-
Ac-IEPD-CHO
a reversible aldehyde caspase-3 inhibitor, bound in extended conformation in the S1-S4 substrate binding sites of caspase-3, binding structure with hydrogen bond and ionic interactions, overview
Ac-LDVPD-CHO
pKi: 7.88/7.66. Little selectivity for caspase-2 over caspase-3
-
Ac-QDTRD-CHO
moderate inhibitory affinity for caspase-2 with approximately the same affinity for caspase-3
-
Ac-WDRAD-CHO
moderate inhibitory affinity for caspase-2 with approximately the same affinity for caspase-3
-
Ac-WEHD-CHO
a reversible aldehyde caspase-3 inhibitor, bound in extended conformation in the S1-S4 substrate binding sites of caspase-3, binding structure with hydrogen bond and ionic interactions, overview
Ac-YVAD-CHO
a reversible aldehyde caspase-3 inhibitor, bound in extended conformation in the S1-S4 substrate binding sites of caspase-3, binding structure with hydrogen bond and ionic interactions, overview
acetyl-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
alpha-fetoprotein
interacts with caspase-3 through precise amino acids, namely loop-4 residues Glu-248, Asp-253 and His-257. alpha-Fetoprotein plays a critical role in the inhibition of the apoptotic signal transduction that mediated by caspase-3
-
Bcl-2
-
an antiapoptotic protein that is localized to the intracellular membrane, nuclear membrane and endoplasmic reticulum, and blocks caspase activation by inhibiting the mitochondrial release of cytochrome c
-
Bcl2-Like12
-
is a nuclear and cytoplasmic oncoprotein that inhibits caspase-3 and apoptosis, mechanism, overview
-
benzyloxycarbonyl-Val-Ala-Asp(OMe)-fluoromethylketone
-
a specific caspase 3 inhibitor
benzyloxycarbonyl-Val-Ala-DL-Asp-fluoromethylketone
-
a general caspase inhibitor
calbindin D28k
-
prevents osteoblast apoptosis by interaction and direct inhibition of caspase-3
-
ethyl 2-amino-6-bromo-4-(1-cyano-2-ethoxy-2-oxoethyl)-4H-chromene-3-carboxylate
-
a BH3 mimetic compound, inhibits activation of procaspase-3
FLICE-inhibitory proteins
-
some isoforms, including FLIPR inhibit Fas-mediated apoptosis by impeding caspase 3 activity as well as poly(ADP-ribose) polymerase cleavage
-
G-CSF
-
a caspase-3 inhibitor that also inhibits the steady increase in cytosolic free Ca2 during neutrophil aging, which is essential for apoptosis
-
glutathione disulfide
-
glutathionylation of caspase can occur at physiologically relevant concentrations of glutathione disulfide and results in the inhibition of caspase activation and activity
hexynoyl-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-Bpa-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
hexynoyl-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
hexynoyl-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-photoLeu-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
hexynoyl-Bpa-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
hexynoyl-photoLeu-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
inhibitor of apoptosis protein
-
IAP, the family members block effector caspase-3 further downstream, which potentially inhibits apoptosis
-
methyl (8-bromo-4-methyl-1,3-dioxo-1,3-dihydro-2H-pyrrolo[3,4-c]quinolin-2-yl)acetate
-
50% inhibition at 0.00046 mM
methyl 3-nitro-5-[[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]carbonyl]benzoate
-
50% inhibition at 104 nM
methyl 3-nitro-5-[[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)amino]carbonyl]benzoate
-
50% inhibition at 66 nM
methyl N-acetyl-3-(pyridin-3-yl)-D-alanyl-N-[[(3S)-1-[(2R)-1-[(3S)-1-methoxy-5-[[(5-methylthiophen-2-yl)carbonyl]oxy]-1,4-dioxopentan-3-yl]amino-1-oxo-3-phenylpropan-2-yl]amino]-5-methyl-1-oxohexan-3-yl]-L-alpha-asparaginate
-
low nanomolar potency against caspase-3 with more than 120fold selectivity over caspase-7
methyl N-[[4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinolin-8-yl]sulfonyl]-D-phenylalaninate
-
50% inhibition at 0.000023 mM
methyl [4-methyl-8-(morpholin-4-ylsulfonyl)-1,3-dioxo-1,3-dihydro-2H-pyrrolo[3,4-c]quinolin-2-yl]acetate
-
50% inhibition at 0.000016 mM
methyl [4-methyl-8-(morpholin-4-ylsulfonyl)-1,3-dioxo-1,3-dihydro-2H-pyrrolo[3,4-c]quinolin-2-yl]propionate
-
50% inhibition at 0.000037 mM
myricetin
-
myricetin directly interacts with the active site of caspase-3 via three hydrogen bonds, via two hydroxyl groups on the B ring of myricetin interacting with Glu123 and the ether oxygen on the C ring interacting with Arg207, and myricetin directly inhibits caspase-3 activity, thereby inhibiting glutamate-induced cell death, but myricetin inhibits glutamate-induced neuronal toxicity by multiple biochemical pathways, e.g. inhibition of NMDA receptor 1 Ser-890 phosphorylation, overview. Molecular docking analysis by Monte Carlo and molecular dynamics simulations
N-(2-hydroxyethyl)-4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonamide
-
50% inhibition at 0.000020 mM
N-(2-methoxyethyl)-4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonamide
-
50% inhibition at 0.000021 mM
N-(2-methoxyphenyl)-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)succinamide
-
50% inhibition at 113 nM, comparison with inhibitory effect on caspase-2, caspase-6, caspase-7, caspase-8, papain, proteasome, trypsin and thrombin
N-(3-ethoxyphenyl)-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)succinamide
-
50% inhibition at 55 nM
N-(3-propyloxyphenyl)-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)succinamide
-
50% inhibition at 71 nM
N-acetyl-3-(pyridin-3-yl)-L-alanyl-N-[(3S)-1-[[(2S)-1-([(2S)-1-carboxy-4-[(2,6-dimethylbenzoyl)oxy]-3-oxobutan-2-yl]amino)-5-methyl-1-oxohexan-2-yl]amino]-5-methyl-1-oxohexan-3-yl]-L-alpha-asparagine
-
low nanomolar potency against caspase-3 with more than 30fold selectivity over caspase-7
N-acetyl-Asp-Glu-Val-Asp-aldehyde
-
a caspase-3 inhibitor, i.e. DEVD-CHO, partially inhibits the DNA fragmentation and growth-inhibition induced by inotodiol
N-acetyl-L-alpha-aspartyl-L-alanyl-N-[(1S)-1-(carboxymethyl)-2-oxo-5-phenylpentyl]-L-valinamide
-
50% inhibition at 2 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
N-acetyl-L-alpha-aspartyl-L-alanyl-N-[(1S)-3-(benzylsulfanyl)-1-(carboxymethyl)-2-oxopropyl]-L-valinamide
-
50% inhibition at 0.5 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxo-3-phenylpropyl]-L-valinamide
-
comparison with inhibition of caspase-7
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxo-4-phenylbutyl]-L-valinamide
-
comparison with inhibition of caspase-7
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxoheptyl]-L-valinamide
-
comparison with inhibition of caspase-7
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxooctyl]-L-valinamide
-
comparison with inhibition of caspase-7
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-4-(2,5-dimethylphenyl)-2-oxobutyl]-L-valinamide
-
comparison with inhibition of caspase-7
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-4-(3-methylphenyl)-2-oxobutyl]-L-valinamide
-
-
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-2-carboxy-1-formylethyl]-L-valinamide
-
50% inhibition at 27 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
N-acetyl-L-alpha-aspartyl-L-valyl-N-[(1S)-2-carboxy-1-[[(4-methylphenyl)(nitroso)amino]methyl]ethyl]-L-alaninamide
-
-
N-acetyl-L-aspartyl-L-valyl-N-[(1S)-2-carboxy-1-[[(4-methylphenyl)(nitroso)amino]methyl]ethyl]-L-alaninamide
-
-
N-allyl-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)succinamide
-
50% inhibition at 44 nM
N-alpha-tosyl-L-lysinyl-chloromethylketone
-
TLCK, a serine protease inhibitor and potent but nonspecific inhibitor of mature caspases, TLCK has no or only slight effect on caspase-3 processing, but TLCK substantially inhibits caspase-3 enzymatic DEVDase activity, but does not prevent cells from death
N-benxylozycarbonyl-tLeu-Asp
-
a peptide adehyde, competitively inhibits human caspase-3 activity in vitro. Z-tLeu-Asp-H impairs apoptosis in human DLD-1 colon adenocarcinoma cells without affecting caspase-8, in vivo effects, overview
N-benxylozycarbonyl-tLeu-Val-Asp
-
a peptide adehyde, competitively inhibits human caspase-3 activity in vitro
N-benxylozycarbonyl-Val-tLeu-Asp
-
a peptide adehyde, competitively inhibits human caspase-3 activity in vitro
N-carbobenzyloxy-D(OMe)E(OMe)VD(OMe)-fluoromethyl ketone
-
a caspase-3 inhibitor
N-propyl-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)succinamide
-
50% inhibition at 59 nM
N-tosyl-L-phenylalaninyl-chloromethylketone
-
TPCK, a serine protease inhibitor and potent but nonspecific inhibitor of mature caspases, enhances caspase-3 processing although it substantially inhibits caspase-3 enzymatic DEVDase activity in HL-60 cells exposed to various cell death inducing stimuli, but does not prevent cells from death, overview
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(4-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[2-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[3-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(morpholin-4-ylsulfonyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-chloro-3-(trifluoromethyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-[(4-methylpiperazin-1-yl)sulfonyl]phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
sodium 4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonate
-
50% inhibition at 0.00014 mM
taurocholate
-
at low concentrations of 0.00001-0.1 mM it increases caspase-3 activity, but at larger doses of 0.5-10 mM it reverses stimulation to inhibition. It inhibits the caspase-3 pathway and prevents ethanol-induced caspase-3 activation leading to inhibition of apoptosis, overview
triptolide
-
a diterpenoid triepoxide derived from the herb Tripterygium wilfordii that is used as a natural medicine in China, activates caspase-3 4-119fold in KB cells, 4-70fold in SCC25 cells, and 7.5-90.5fold in OEC-M1 cells, all cancer cells, within 2 days, overview
VhhCasp31
-
reduces the enzyme activity by 39% at 0.0047 mM and by 85.5% at 0.0145 mM, which is a concentration three times that of caspase 3, the VHH proteins, expresed in SHSY-5Y cells and isolated from heavy chain antibody variable domain, i.e. VHH phage display library, are specific to caspase 3 and antagonist and agonist of apoptosis, effects of transiently-expressed VhhCasp31 and VhhCasp32 intrabodies on oxidative-stress-induced apoptosis in SHSY-5Y cells, overview
-
X inhibitor of apoptosis protein
-
recombinant, a member of the inhibitor of apoptosis protein family, inhibits caspase-3
-
Z-IETD-fluoromethylketone
-
a caspase 8 specific inhibitor, delays the activation of caspase 3 and caspase 9 significantly
ZINC13341044
screening of caspase-3 inhibitors from natural molecule database using e-pharmacophore and docking studies
ZINC13507846
screening of caspase-3 inhibitors from natural molecule database using e-pharmacophore and docking studies
[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl](oxo)acetyl chloride
-
-
3-({2-[5-tert-butyl-3-{[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino}-2-oxopyrazin-1(2H)-yl]butanoyl}amino)-5-[methyl(pentyl)amino]-4-oxopentanoic acid
-
a chemical and reversible caspase-3 inhibitor, M867 reduces clonogenic survival in H460 lung cancer cells
3-({2-[5-tert-butyl-3-{[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino}-2-oxopyrazin-1(2H)-yl]butanoyl}amino)-5-[methyl(pentyl)amino]-4-oxopentanoic acid
-
a chemical and reversible caspase-3 inhibitor, M867 with ionizing radiation in an in vivo mouse hind limb lung cancer model is well tolerated, and produces a significant tumor growth delay compared to radiation alone
M826
-
IC50: 0.00003 mM; i.e. (R,S)-[[(2S)-2-[5-tert-butyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]butanoyl]amino]-5-[hexyl(methyl)amino]-4-oxopentanoic acid hydrochloride, selectively and potently inhibits both caspase-3 enzymatic activity and apoptosis in cultured cell in vitro
M826
-
IC50 for enzyme from cerebellar granule neuron: 0.00005 mM. IC50 for enzyme from cortical neuron: 0.00012 mM; i.e. (R,S)-[[(2S)-2-[5-tert-butyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]butanoyl]amino]-5-[hexyl(methyl)amino]-4-oxopentanoic acid hydrochloride, selectively and potently inhibits both caspase-3 enzymatic activity and apoptosis in cultured cell in vitro
N-carbobenzyloxy-DEVD-fluoromethyl ketone
-
effects on the activation of caspase-3 through cell infection with Leptospira interrogans
N-carbobenzyloxy-DEVD-fluoromethyl ketone
-
a caspase-3-specific inhibitor, that efficiently reduces rhein-induced apoptosis by 61% at 0.01 mM resulting in 28% apoptotic cells, overview
N-carbobenzyloxy-DEVD-fluoromethyl ketone
-
effects on the activation of caspase-3 through cell infection with Leptospira interrogans
N-carbobenzyloxy-VAD-fluoromethyl ketone
-
a generic caspase inhibitor, that effectively blocks FasL-induced cleavage of caspase-3 and completely prevents FasL-induced degradation of Grx1
NO
-
NO supplied by exogenous NO donors serves in vivo as an antiapoptotic regulator of caspase activity via S-nitrosation of the Cys163 residue of caspase-3
survivin
-
inhibits processing of procaspase-3 and specifically binds the active form of caspase-3 through a baculovirus inhibitor of apoptosis, IAP, repeat domain
-
additional information
-
screening of caspase-3 inhibitors using a dual-step fluorescence resonance energy transfer-based quenching assay for, method development with fluorescent europium(III)-chelate-doped nanoparticle donors coated with streptavidin in conjunction with a dual-labeled caspase-3-specific peptide substrate modified with a biotinyl moiety, overview
-
additional information
-
N-propyl- and N-butyl isatins, as well as the corresponding terminal alcohols and regioisomeric fluorobutyl derivatives are excellent inhibitors, fluorinated N-benzyl isatins as well as trifluoroalkyl and difluoroalkyl derivatives are moderate inhibitors, while isatins bearing different alkylether groups at N-1 are very weak or not active as inhibitors of caspases-3, inhibitory potencies and structure-activity relationships, overview
-
additional information
-
insulin inhibits caspase-3 activity 30-60% in renal tubular epithelial cells via the PI3-kinase/Akt pathway, insulin deprivation for 24 or 48 h leads to a significant increase of the caspase-3 enzyme activity by 15% and 58%, respectively
-
additional information
-
inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 activation
-
additional information
-
caspase-3 is S-nitrosylated under basal conditions to prevent activation
-
additional information
-
processing of caspase-3 is affected only negligibly in cells treated with etoposide or N6-(2-isopentenyl)adenosine
-
additional information
-
caspase-3 inhibitory activity of 1,3-dioxo-4-methyl-2,3-dihydro-1h-pyrrolo[3,4-c] quinolines, quantitative structure-activity relationships, overview
-
additional information
-
ischemic/reperfusion in brain leads to increased release of cytochrome c from mitochondria and activation of caspase-3, ischemic preconditioning with 6,7,8,9-tetrahydro-5-nitro-1 H-benz[g]indole-2,3-dione-3-oxime, i.e. NS102, and ischemic tolerance can diminish the activation of caspase-3, overview
-
additional information
-
survivin, a member of the inhibitor of apoptosis protein family, does not inhibit caspase-3
-
additional information
-
structure-based drug design approach, synthesis of beta-strand urazole ring-containing irreversible peptidomimetic compounds. Z-VAD-fmk and the peptidomimetic inhibitors inhibit caspase-3 via a three-step kinetic mechanism, i.e. two rapid equilibrium steps followed by a relatively fast inactivation step, caspase-inhibitor interactions, overview
-
additional information
-
isatin 1,2,3-triazoles as potent inhibitors against caspase-3 via competitive inhibitory mechanism, synthesis by the Huisgen cycloaddition reaction, inhibitory potencies, overview
-
additional information
-
Z-LEHD-fluoromethylketone, a caspase 9 specific inhibitor, does not affect caspase 3 activation
-
additional information
-
1,2-benzisothiazol-3(2H)-one, lacks caspase-3 inhibitory activity
-
additional information
-
molecules with psi(CH2NH) or triazole uncleavable peptide bond do not show any inhibition of caspase activity without irradiation. When the samples are irradiated, the psi(CH2NH) peptides with benzophenone or diazirine photocrosslinkers show complete inhibition
-
additional information
-
interleukin-1 downregulates caspase-3 expression and reduces apoptsis within the gastrointestinal crypts
-
additional information
-
inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 activation
-
additional information
-
Phyllanthus amarus inhibits cell growth and induces apoptosis in Dalton's lymphoma ascites cells through activation of caspase 3 and downregulation of bcl-2, overview
-
additional information
inhibition of caspase 3 activity leads to a profound disruption in skeletal muscle regeneration with an accumulation of satellite cells within the niche
-
additional information
-
thiorphan, a specific NEP/CD10 inhibitor, causes downregulation of procaspase-3 mRNA levels and suppression of caspase-3 activity in a neurokinin-1 receptor-dependent manner. The effect is abrogated by the NK1R antagonist (S)1-{2-[3(3-4-dichlorophenyl)-1-(3-iso-propoxyphenylacetyl)-piperidine-3-yl]ethyl}-4-pheny-1-azoniabicyclo[2.2.2]octane, chloride, i.e. SR140333, overview
-
additional information
-
IkappaB-antisense oligonucleotides inhibit caspase-9 but also caspase-3 activity
-
additional information
-
no inhibitory activity of compounds 3-hydroxyl-2-N-iso-butyryl-anthranilamide, anthranilamide, 8-hydroxyl-4(3H)-quinazoline, and 8-hydroxyl-2-methyl-4(3H)-quinazoline from Streptomyces sp., a mangrove actinomycete, strain 061316
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
azinomycin epoxide
-
i.e. (2S,3S)-benzyl 3,4-epoxy-2-(3-methoxy-5-methyl-1-naphthoyloxy)-3-methylbutanamide, leads to activation and apoptosis in THP-1 cells in a p53-independent manner, while human apoptosis signal-regulating kinase 1, ASK1, is highly required for caspase-3 activation by (2S,3S)-benzyl 3,4-epoxy-2-(3-methoxy-5-methyl-1-naphthoyloxy)-3-methylbutanamide, transient expression of the dominant-negative human ASK1 with kinase-dead domain in THP-1 cells abolishes the caspase-3 activating effect of azinomycin epoxide, overview
C2-ketoCer
-
i.e. (2S,4E)-2-acetylamino-3-oxo-4-octadecen-1-ol, a ceramide analogue, activates caspase-3 and induces apoptosis
carboxyfluorescein-valyl-alanyl-aspartic-acid fluoromethyl ketone
-
the FAM-peptide irreversibly binds to active caspases
cisplatin
-
with or without pre-treatment with HA14-1 it increases the cleavage of caspase-3
homocysteine
-
induces the enzyme activation 2.5fold and 4fold in endothelial progenitor cells at 0.1 mM and 0.2 mM, respectively. Vitamin B6, and B9 significantly impair homocysteine-mediated EPC caspase-3 activation in vitro, and inhibitor N-carbobenzyloxy-VAD-fluoromethyl ketone highly reduces the activating effect, overview
Lactic acid
-
induces the activation of caspase-3 in keratinocytes, the activation can be inhibited by N-carbobenzyloxy-VAD-fluoromethyl ketone, overview
paclitaxel
-
pre-treatment of cells with HA14-1 followed by paclitaxel induces cleavage of pro-caspase-3 to active form
pancreatic derived factor
-
islet specific cytokine, capable of inducing apoptosis, increases levels of cleaved CASP3 in beta-TC3 cells
-
staurosporine
-
in myotubes, staurosporine increases proteasome activity by 38% and stimulates cleavage of proteasome subunits, Rpt2, Rpt6, and Rpn2. Rpt5 and Rpn10 subunits are not cleaved in staurosporine-treated myotubes
TNF-alpha/irradiation
-
leads to an increase of caspase-3, administration of TNF-alpha to non-irradiated hepatocytes does not lead to an increased activity of caspase-3, administration of TNF-alpha to non-irradiated hepatocytes does not lead to an increased activity of caspase-3. Irradiation induces TNF-alpha-mediated activation of caspase-3, and apoptosis in hepatocytes. Apoptosis induction is prevented by IkappaB antisense oligonucleotides mediated by suppression of caspases-3 activation, overview
-
trichothecin
-
trichothecin increases caspase-9, EC 3.4.22.62, expression and caspase-3 activity, and induces apoptosis of HepG2 cells via caspase-9 mediated activation of the mitochondrial death pathway
VhhCasp32
-
increases the enzyme activity by 38% at 0.0047 mM, the VHH proteins, expresed in SHSY-5Y cells and isolated from heavy chain antibody variable domain, i.e. VHH phage display library, are specific to caspase 3 and antagonist and agonist of apoptosis, effects of transiently-expressed VhhCasp31 and VhhCasp32 intrabodies on oxidative-stress-induced apoptosis in SHSY-5Y cells, overview
-
xanthorrhizol
-
a natural sesquiterpenoid compound isolated from the rhizome of Curcuma xanthorrhizza, modulates MDA-MB-231 cell apoptosis through the mitochondria-mediated pathway subsequent to the disruption of mitochondrial transmembrane potential, release of cytochrome c, activation of caspase-3 and caspase-9, and the modulation of PARP-1 protein, overview
cytochrome c
-
release of cytochrome c in vivo leads to increased caspase-3 activation in Daltons lymphoma cells
cytochrome c
-
forebrain ischemia causes release of cytochrome c from mitochondria and translocation to the nucleus, which induces caspase-3 activation
additional information
-
lipopeptide from the producing strain Bacillus natto TK-1, from the traditional Japanese food natto, induces caspase-3 activation
-
additional information
-
camptothecin incubation results in an approximately 3fold increase of the caspase-3 activity in renal tubular epithelial cells associated with a significant decrease of cell number
-
additional information
-
6-(1-oxoallkyl)-5,8-dimethoxy-1,4-naphthoquinone-S17, i.e. DMNQ-S17, induces caspase-3 expression and activation via inhibition of NF-kappaB activation, and apoptosis, apoptotic mechanism, overview
-
additional information
-
protein expression and activity of caspase-3 is upregulated by gene E1A, i.e. human adenovirus type 5 early region 1A, expression
-
additional information
-
alphaB-crystallin knockdown sensitizes Bcl2L12-expressing astrocytes toward apoptosis in association with increased effector caspase activity
-
additional information
-
alpha-trifluoromethyl acyloins TF2 and TF3, i.e. CF3CH(OH)COPh and CF3CH(OH)COCH2Ph, fail to activate caspase-3 in both HSC-2 and HSC-4 cells during 4-24 hours treatment, however, TF2 and TF3 induce apoptotic cell death in human submandibular gland carcinoma cells
-
additional information
-
In some cells, active caspase-8 is sufficient to activate caspase-3 directly. In other cells, however, caspase-8 indirectly mediates caspase-3 activation by cleaving the proapoptotic Bcl-2 family member Bid, which induces mitochondrial cytochrome c release. Leptospira interrogans induces apoptosis in macrophages and hepatocytes via caspase-8- and caspase-3-dependent pathways
-
additional information
-
engagement of Fas causes a rapid activation of caspase-3, induction of caspase-3 by Fas ligand, FasL, overview. Increased S-glutathionylation of Fas, caspase-3 activity, and cell death in cells lacking Grx1
-
additional information
-
mycotoxin citrinin triggers caspase-3 activity, which is significantly reduced in presence of MAPK inhibitors
-
additional information
-
caspase-3 activity is increased in cells with inhibited nectrin-1 or deleted nectrin-1 receptors, overview
-
additional information
-
procaspase-8 is cleaved to 41 and 43 kDA fragments for activation, overview
-
additional information
-
ischemic/reperfusion in brain leads to increased release of cytochrome c from mitochondria and activation of caspase-3, ischemic preconditioning and ischemic tolerance can diminish the activation of caspase-3, overview
-
additional information
-
caspase-3 is activated downstream of the death receptor signaling or via death receptor-independent pathway
-
additional information
-
activation dynamics of caspase 3. Caspase 3 is activated rapidly. During H2O2-induced apoptosis, caspase 3 is activated directly through caspase 8 and not through the mitochondria-dependent caspase 9 activation
-
additional information
-
cordycepin induces caspase-3 protein expression, and apoptosis in MA-10 mouse Leydig tumor cells through a caspase-3 dependent pathway, overview
-
additional information
-
caspase-3 activation and apoptosis are increased under irradiation stress, but interleukin-1 does prevent it when used in pretreatment, interleukin-1beta pretreatment causes reduced caspase-3 activation, overview
-
additional information
-
In some cells, active caspase-8 is sufficient to activate caspase-3 directly. In other cells, however, caspase-8 indirectly mediates caspase-3 activation by cleaving the proapoptotic Bcl-2 family member Bid, which induces mitochondrial cytochrome c release. Leptospira interrogans induces apoptosis in macrophages and hepatocytes via caspase-8- and caspase-3-dependent pathways
-
additional information
-
alphavirus Semliki Forest virus infection initiates apoptosis with increased caspase-3 activation, and interferon synthesis in embryonic fibroblasts, overview
-
additional information
-
caspase-3 activity within cells is slightly increased after treatment of free heparin for 2 day, internalized heparin triggers apoptosis-inducing stimuli for activation of caspases and subsequent apoptotic cell death
-
additional information
-
benzene, tendency to increase caspase-3 expression after 12 days of oral benzene treatment to p53KO mice
-
additional information
-
lipoic acid has no effect on caspase-3 activity
-
additional information
-
N-methyl-D-aspartate induces caspase-3 activation, mechanism, overview, autocamtide-2-related inhibitory peptide attenuates caspase-3 activation
-
additional information
-
ethanol and acetylsalicylic acid induce caspase-3 activation, which is inhibited by taurocholate at low concentrations of 0.00001-0.1 mM
-
additional information
-
caspase-3 is induced by physical activiy and energy intake, regulation, overview
-
additional information
-
irradiation induces caspase-3 activity about 5fold
-
additional information
-
direct activation of procaspase-3 by caspase-9 and caspase-8 in type I cells through proteolytic cleavage
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0016
5'-tetramethylrhodamine-5(6)-carboxamide-DEVD-cyanine 5
-
pH and temperature not specified in the publication
0.0004
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Ala-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0015
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Ala-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0008
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Asn-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0004
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Asn-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0006
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Glu-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0006
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Gly-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0003
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Gly-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0002
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0008
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0002
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Val-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0018
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Val-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
additional information
additional information
-
stopped-flow and steady-state kinetic kinetics
-
0.0144
acetyl-DEVD-7-amido-4-methylcoumarin
-
partially purified enzyme from Jurkat T cells
5.6
acetyl-DEVD-7-amido-4-methylcoumarin
-
pH 7.4, presence of 5 mM 2-mercaptoethanol
10.4
acetyl-DEVD-7-amido-4-methylcoumarin
-
pH 7.4, presence of 5 mM dithiothreitol
0.0048
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant DELTA176-181, pH 4.75, 37°C
0.0088
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant DELTA176-181, pH 7.2, 37°C
0.0122
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
wild-type, pH 4.75, 37°C
0.0138
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
wild-type, pH 7.2, 37°C
0.0163
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant D179A, pH 4.75, 37°C
0.0335
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant D179A, pH 7.2, 37°C
0.002
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant DELTA176-181, pH 4.75, 37°C
0.0069
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant DELTA176-181, pH 7.2, 37°C
0.008
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
wild-type, pH 4.75, 37°C
0.0097
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
wild-type, pH 7.2, 37°C
0.013
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant D179A, pH 4.75, 37°C
0.0255
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant D179A, pH 7.2, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0217
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Ala-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0183
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Ala-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.017
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Asn-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.013
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Asn-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.015
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Glu-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.00917
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Gly-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.0083
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Gly-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.023
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.015
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.028
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Val-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.023
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Val-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
0.08
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant DELTA176-181, pH 4.75, 37°C
0.33
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
wild-type, pH 4.75, 37°C
1.37
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant D179A, pH 4.75, 37°C
1.54
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant DELTA176-181, pH 7.2, 37°C
3.5
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant D179A, pH 7.2, 37°C
6.01
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
wild-type, pH 7.2, 37°C
19.56
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant D179A, pH 7.2, 37°C
0.03 - 0.55
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
wild-type, pH 7.2, 37°C
0.06
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant DELTA176-181, pH 4.75, 37°C
0.16
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
wild-type, pH 4.75, 37°C
1.1
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant D179A, pH 7.2, 37°C
1.1
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant D179A, pH 4.75, 37°C
1.43
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant DELTA176-181, pH 7.2, 37°C
7.08
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
wild-type, pH 7.2, 37°C
19.04
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
mutant D179A, pH 7.2, 37°C
additional information
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
wild-type, pH 7.2, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
56.7
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Ala-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
11.7
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Ala-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
20
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Asn-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
33.3
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Asn-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
25
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Glu-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
13.3
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Gly-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
28.3
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Gly-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
96.7
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
20
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
135
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Val-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
13.3
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Val-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000165
(3S)-3-[[(2R)-2-[3-[(naphthalen-2-ylcarbonyl)amino]-2-oxopyridin-1(2H)-yl]-2-phenylacetyl]amino]-4-oxo-5-phenoxypentanoic acid
-
Ki-value is calculated from the initial rates
0.0021
(4S,7S,10S,13S)-7-(2-carboxyethyl)-4-(carboxymethyl)-13-(cyclobutylcarbonyl)-10-(1-methylethyl)-2,5,8,11-tetraoxo-3,6,9,12-tetraazapentadecan-15-oic acid
-
-
0.012
(R)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
pH 7.5, 30°C
0.0000012
(S)-1-benzyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
pH 7.5, 30°C
0.000019
(S)-1-[(tert-butyloxycarbonyl)methyl]-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
pH 7.5, 30°C
0.00016
(S)-3-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-pyridin-2-ylmethyl]sulfamoyl]benzoic acid
-
pH 7.4
0.0017
(S)-3-[[6-(benzenesulfonylamino-methyl)pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.00047
(S)-3-[[6-[(3-acetylsulfamoyl-benzenesulfonylamino)-methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.0017
(S)-3-[[6-[(3-methanesulfonyl-benzenesulfonylamino)-methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.0013
(S)-3-[[6-[(3-methanesulfonylamino-benzenesulfonylamino)methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.0014
(S)-3-[[6-[(3-methanesulfonylaminocarbonyl-benzenesulfonylamino)methyl]-pyridine-3-carbonyl]amino]-4-oxobutyric acid
-
pH 7.4
0.0023
(S)-3-[[6-[(4-hydroxy-benzenesulfonylamino)methyl]-pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.0019
(S)-3-[[6-[(4-methanesulfonylamino-benzenesulfonylamino)methyl]pyridien-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.00044
(S)-4-oxo-3-[[6-[[3-(1H-tetrazol-5-yl)benzenesulfonylamino]methyl]pyridine-3-carbonyl]amino]butyric acid
-
pH 7.4
0.0004
(S)-4-oxo-3-[[6-[[3-(5-oxo-4,5-dihydro[1,2,4]oxadiazol-3-yl)benzenesulfonylamino]methyl]pyridien-3-carbonyl]amino]butyric acid
-
pH 7.4
0.00021
(S)-4-[[4-(hydroxy-3-methyl-benzenesulfonylamino)methyl]thiophene]-2-carboxylic acid [3-(2-chloro-benzylsulfanyl)-1-ethyl-2-oxo-propyl]amide
-
pH 7.4
0.00006
(S)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
pH 7.5, 30°C
0.000015
(S)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
pH 7.5, 30°C
0.00016
(S)-5-[[3-(1-carboxymethyl-2-oxo-ethylcarbamoyl)isooxazol-5-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00006
(S)-5-[[3-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]isoxazol-5-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.0025
(S)-5-[[4-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00029
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-4-methyl-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.0125
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-furan-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00048
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-pyrazin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00007
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiazol-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00012
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.004
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-3-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00005
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00002
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyrimidin-2-ylmethyl]sulfamoyl]-2-hydroxybenzoic acid
-
pH 7.4
0.00019
(S)-5-[[5-(1-carboxymethyl-3-methylsulfanyl-2-oxo-propylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00002
(S)-5-[[5-[1-carboxymethyl-2-oxo-3-(pyridin-3-ylmethylsulfanyl)propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00003
(S)-5-[[5-[1-carboxymethyl-2-oxo-3-(pyridin-4-ylmethylsulfanyl)propylcarbamoyl]thiophen-2-ylmethyl]-sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00004
(S)-5-[[5-[1-carboxymethyl-3(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]-4-methyl-thiophen-2-ylmethyl]-sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.004
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]furan-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00009
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyrazin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00003
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00002
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyrimidin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00003
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiazol-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00002
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00027
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-3-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00024
(S)-5-[[5-[1-carboxymethyl-5-(2-chloro-phenyl)-2-oxopentylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.000011
1-methyl-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
Ki-value is calculated from the initial rates
0.000077
3,3-dimethyl-8-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-3,4-dihydropyrimido[1,2-a]indol-10(2H)-one
-
Ki-value is calculated from the initial rates
0.0000161
5-([(2S)-2-[(pyridin-3-yloxy)methyl]pyrrolidin-1-yl]sulfonyl)-1H-indole-2,3-dione
-
Ki-value is calculated from the initial rates
0.0000025
5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-phenyl-1H-indole-2,3-dione
-
Ki-value is calculated from the initial rates
0.00029
5-[[5-[1-carboxymethyl-2-(7-methyl-benzoxazol-2-yl)-2-oxo-ethylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00038
5-[[5-[1-carboxymethyl-2-[5-(2,6-dichloro-phenyl)-oxazol-2-yl]-2-oxo-ethylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.000478
8-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-3,3-dimethyl-3,4-dihydropyrimido[1,2-a]indol-10(2H)-one
-
Ki-value is calculated from the initial rates
0.0015
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxo-3-phenylpropyl]-L-valinamide
-
-
0.0035
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxo-4-phenylbutyl]-L-valinamide
-
-
0.0011
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxoheptyl]-L-valinamide
-
-
0.0013
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxooctyl]-L-valinamide
-
-
0.0002
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-4-(2,5-dimethylphenyl)-2-oxobutyl]-L-valinamide
-
-
0.0007
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-4-(3-methylphenyl)-2-oxobutyl]-L-valinamide
-
-
0.002
N-acetyl-L-alpha-aspartyl-L-valyl-N-[(1S)-2-carboxy-1-[[(4-methylphenyl)(nitroso)amino]methyl]ethyl]-L-alaninamide
-
pH 7.5, 30°C
additional information
additional information
-
Ki-value for enzyme from THP.1 cells with the inhibitor Ac-DEVD-aldehyde is below 1 nM
-
additional information
additional information
-
inhibition kinetics, first-order inhibition kinetics and two-step irreversible inhibition mechanism
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0142
(3S)-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00066
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(2-phenylethyl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00681
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(pyridin-3-yl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00524
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-[2-[(thiophen-2-ylacetyl)amino]ethyl]-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00505
(3S)-3-([[2-(3-carboxypropyl)-8-(2-[[(4-chlorophenyl)acetyl]amino]ethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0172
(3S)-3-([[2-[2-[(1H-benzimidazol-6-ylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00754
(3S)-3-([[2-[2-[(cyclohexylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0134
(3S)-3-[[(2-[4-carboxy-2-[(phenylacetyl)amino]butyl]-1,3-dioxo-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl)carbonyl]amino]-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0084
(3S)-5-(2,6-difluorophenoxy)-3-([[(2-methoxyphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0252
(3S)-5-(2,6-difluorophenoxy)-3-([[(3-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00967
(3S)-5-(2,6-difluorophenoxy)-3-([[(4-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00347
(3S)-5-fluoro-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00203
(3S)-5-[(2,6-dichlorobenzoyl)oxy]-3-[([1,3-dioxo-2-[2-(1H-tetrazol-5-yl)ethyl]-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl]carbonyl)amino]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.018
(R)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
Homo sapiens
IC50: 0.018 mM
0.0055
(R)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 0.0055 mM
0.000044
(S)-(+)-5-[1-[2-(thiophenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 44 nM
0.000017
(S)-1-((1-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-1H-1,2,3-triazol-4-yl)methyl)-5-((2-(methoxymethyl)pyrrolidin-1-yl)sulfonyl)indoline-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000066
(S)-1-(11,11-difluoroundecyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0005
(S)-1-(2-fluoroallyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00184
(S)-1-(2-fluoroethyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0000133
(S)-1-(3-chloro-2-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00009
(S)-1-(3-chloropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000025
(S)-1-(3-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00512
(S)-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000078
(S)-1-(3-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000041
(S)-1-(4-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00003
(S)-1-(4-hydroxybutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0000042
(S)-1-(4-pyridinylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
Homo sapiens
IC50: 4.2 nM
0.00017
(S)-1-(carboxymethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 170 nM
0.0000052
(S)-1-(cyclohexylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
Homo sapiens
IC50: 5.2 nM
0.0000046
(S)-1-allyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 4.6 nM
0.0000025
(S)-1-benzyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 2.5 nM
0.00003
(S)-1-methyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 30 nM
0.0000053
(S)-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-isatin
Homo sapiens
-
37°C
0.0000031
(S)-1-[(tert-butyloxycarbonyl)methyl]-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 3.1 nM
0.1
(S)-1-[3-(3-fluoropropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
above, 37°C
0.0609
(S)-1-[3-(3-hydroxypropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00943
(S)-1-[3-[3-(2-fluoroethoxy)propoxy]propyl]-5-[1-(2-methoxymethylpyrrolidinyl)-sulfonyl]isatin
Homo sapiens
-
37°C
0.0068
(S)-3,3-difluoro-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
Homo sapiens
-
37°C
0.1
(S)-3,3-difluoro-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
Homo sapiens
-
above, 37°C
0.000043
(S)-3,5-bis-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.1
(S)-3-[3-[5-(1-(2-methoxymethylpyrrolidinyl)sulfonyl)-2,3-dioxoindolin-1-yl]propoxy]-propyl methanesulfonate
Homo sapiens
-
above, 37°C
0.000187
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propanoic acid
Homo sapiens
-
37°C
0.00023
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propyl methanesulfonate
Homo sapiens
-
37°C
0.000191
(S)-4-fluorobenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000082
(S)-4-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000056
(S)-4-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]butyl 4-methyl-benzenesulfonate
Homo sapiens
-
37°C
0.00012
(S)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
Homo sapiens
IC50: 120 nM
0.000359
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,3,3-trifluoropropyl)isatin
Homo sapiens
-
37°C
0.000083
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,4,4-trifluorobut-3-enyl)isatin
Homo sapiens
-
37°C
0.000213
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(4,4,4-trifluorobutyl)isatin
Homo sapiens
-
37°C
0.00017
(S)-5-[1-[(2-methoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 170 nM
0.00007
(S)-5-[1-[(2-tert-butoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 70 nM
0.000031
(S)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 31 nM
0.000044
(S)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 44 nM
0.00014
(S)-5-[1-[2-(phenylaminocarbonyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 140 nM
0.00041
(S)-5-[1-[[2-(dimethylamino)carbonyl]pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 410 nM
0.000245
1-(3-oxo-1,2-benzothiazol-2(3H)-yl)-4-(thiophen-2-yl)butane-1,4-dione
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.001
1-methyl-5-nitro-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000136
1-[[1-(2,3-dihydro-1,4-benzodioxin-6-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.0000167
1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000023
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000136
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.0002217
2-(1,3-dihydro-2-benzofuran-5-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000000203
2-(2,6-dihydroxyphenyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000729
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(1H-pyrrol-1-yl)phenyl]acetamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000501
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(pyridin-2-yl)phenyl]acetamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001084
2-(3-phenylpropanoyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001816
2-(4-phenylbutanoyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003061
2-(5-phenylpentanoyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5,temperature not specified in the publication
0.0001406
2-(biphenyl-4-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000008
2-(chloroacetyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0002646
2-(naphthalen-2-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002921
2-(phenylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0322
2-(thiophen-2-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000000622
2-amino-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.00000019
2-[(2,6-dihydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.001926
2-[(2-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001857
2-[(2-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000000425
2-[(2-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0002186
2-[(2-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001999
2-[(2-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0006543
2-[(3,4-dichlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000263
2-[(3,5-diamino-4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0002719
2-[(3-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.008985
2-[(3-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000548
2-[(3-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003392
2-[(3-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002151
2-[(4-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.001196
2-[(4-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003263
2-[(4-hydroxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000033
2-[(4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.001344
2-[(4-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002143
2-[(4-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000473
2-[3-(2-chlorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001297
2-[3-(2-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001357
2-[3-(2-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000877
2-[3-(3-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000349
2-[3-(3-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000095
2-[3-(3-methylphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000569
2-[3-(4-chlorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001116
2-[3-(4-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000497
2-[3-(4-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000119
2-[3-(4-methylphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003897
2-[4-(4-methoxyphenyl)butanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002659
2-[4-(4-methylphenyl)butanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001266
2-[4-(thiophen-2-yl)butanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000085
3-oxo-N-(1-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.00004904
3-oxo-N-(3-phenylpropyl)-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000076
3-oxo-N-phenyl-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.00004939
3-oxo-N-[2-(pyridin-2-yl)ethyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00003105
3-oxo-N-[2-(thiophen-2-yl)ethyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00009792
3-oxo-N-[4-(piperidin-1-yl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000221
3-oxo-N-[4-(pyridin-2-yl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00082
3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.000988
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0012
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-5-(2,6-difluorophenoxy)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00058
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-5-fluoro-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00011
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0208
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-5-(2,6-difluorophenoxy)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00035
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-5-fluoro-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00084
3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00111
3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.000000228
4-methyl-2-(1-methylethyl)-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000324
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(1,3-thiazol-2-yl)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000446
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(2,4,6-trihydroxyphenyl)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000124
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(phenylamino)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000243
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-[(2,4,6-trihydroxyphenyl)amino]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.00000161
4-[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl]benzoic acid
Homo sapiens
-
-
0.00913
4-[5-([(3S)-1-[(2,6-dichlorobenzoyl)oxy]-2,5-dioxohexan-3-yl]carbamoyl)-1,3-dioxo-8-(thiophen-2-yl)-5,8-dihydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-2(3H)-yl]butanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0025
5-(2,6-difluorophenoxy)-3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0257
5-(2,6-difluorophenoxy)-3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0471
5-(2,6-difluorophenoxy)-3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0000005
5-([(2R)-2-[(2,4-difluorophenoxy)methyl]pyrrolidin-1-yl]sulfonyl)-1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00123
5-fluoro-3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00112
5-fluoro-3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00129
5-fluoro-3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.000018
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-4-yl]methyl)-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000267
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-5-yl]methyl)-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000009
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000021
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000103
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000243
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-4-yl)ethyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000207
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-5-yl)ethyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000044
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00007
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000021
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000213
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00012
5-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000044
5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00012
6-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
37°C
0.008093
N-(2-bromophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000206
N-(2-fluorobenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.01627
N-(2-fluorophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000088
N-(2-methoxybenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.004167
N-(2-methoxyphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.009823
N-(2-nitrophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.009628
N-(3-bromophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000241
N-(3-fluorobenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000438
N-(3-fluorophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000074
N-(3-methoxybenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.001167
N-(3-methoxyphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.0004307
N-(4-benzoylphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.003071
N-(4-bromophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000115
N-(4-fluorobenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000593
N-(4-fluorophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.1
N-(4-iodophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 7.5 and 22°C
0.00004
N-(4-methoxybenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.01071
N-(4-methoxyphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.04674
N-(5-methylpyridin-2-yl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00008055
N-(furan-2-ylmethyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000023
N-acetyl-3-(pyridin-3-yl)-L-alanyl-N-[(3S)-1-[[(2S)-1-([(2S)-1-carboxy-4-[(2,6-dimethylbenzoyl)oxy]-3-oxobutan-2-yl]amino)-5-methyl-1-oxohexan-2-yl]amino]-5-methyl-1-oxohexan-3-yl]-L-alpha-asparagine
Homo sapiens
-
at pH 7.4 and 22°C
0.04
N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone
Homo sapiens
pH 7.4, 37°C
0.04474
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.06096
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.05149
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.02508
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.6
0.02926
N-[(4-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.01356
N-[2-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002697
N-[2-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001808
N-[3-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000555
N-[3-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00006201
N-[4-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00005685
N-[4-(morpholin-4-yl)benzyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000115 - 0.0001063
N-[4-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
0.0007834
N-[4-(morpholin-4-ylsulfonyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.02205
N-[4-chloro-3-(trifluoromethyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.0000606
N-[4-[(4-methylpiperazin-1-yl)sulfonyl]phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000000008
[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl](oxo)acetyl chloride
Homo sapiens
-
-
0.000031
3-oxo-N-(2-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000031
3-oxo-N-(2-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.00012
M826
Mus musculus
-
IC50 for enzyme from cerebellar granule neuron: 0.00005 mM. IC50 for enzyme from cortical neuron: 0.00012 mM
0.0757
N-acetyl-DEVD-CHO
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00004153
N-benzyl-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000086
N-benzyl-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.00000115
N-[4-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001063
N-[4-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
relative caspase-3 activity in nectrin-1-expressing and nectrin-1-deficient lung cancer cells, overview
additional information
-
activities in KB, SCC25 and OEC-M1 cells in presence and absence of tripolide
additional information
-
caspase-3 activity in Semliki Forest virus-infected cells, overview
additional information
-
caspase-3 activity in healthy hippocampus, hippocampus after 8 min of transient forebrain ischemia, and after 3 days of reperfusion, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.4
-
assay at
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
37
-
assay at
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
647606, 647607, 647609, 647610, 647612, 647614, 647616, 647617, 647618, 647619, 647620, 647623, 647626, 647627, 647628, 647629, 647634, 647635, 647636, 647637, 647644, 667192, 667954, 668206, 668482, 668632, 669306, 678060, 678100, 678208, 678321, 679149, 679154, 679732, 680803, 681528, 681558, 681721, 682802, 682919, 695539, 695620, 695622
-
-
brenda
-
695681, 695950, 695963, 696019, 696717, 696749, 696872, 696934, 697054, 697055, 697139, 697224, 697581, 697769, 698142, 698196, 698258, 698346, 698767, 698791, 699097, 699113, 699135, 699212, 699228, 699346, 699643, 699877, 699914, 699937, 699974, 700291, 700479, 700538, 700544, 700596, 700881, 700938, 701099, 701188, 701309, 707972, 708166, 709751, 710588, 710684, 717272, 717337, 717462, 717470, 717539
-
-
brenda
-
-
-
brenda
commercial preparation, recombinant full-length enzyme expressed in Escherichia coli
-
-
brenda
-
647608, 647612, 647629, 668093, 668726, 680420, 681682, 695618, 697784, 698140, 698258, 699298, 699790, 700600, 700685, 700881, 717792, 731594
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
overexpressing Bcl2-Like12 nuclear and cytoplasmic oncoprotein
brenda
procaspase-3 level is elevated 2fold to 5fold in preovulatory, compared to prehierarchal follicle granulosa cells
brenda
-
emodin induces apoptosis through caspase 3-dependent pathway in HK-2 cells
brenda
-
hippocampal cell line, during glutamate-induced apoptotic cell death, glutamate induces activation of calpain, and translocation of mitochondrial apoptosis inducing factor AIF to cytosol and nuclei. Enzyme is not involved
brenda
-
the active caspase-3 expression is higher in the anterior pole of the lens
brenda
-
expression patterns of the major caspases, CASP3, 6, 7, 8, 9, and 10, and inhibitor of apoptosis proteins, survivin, CIAP1, CIAP2, XIAP, and livin, overview
brenda
-
epithelial acinar cells, nonobese diabetic mouse acinar cells at 16 weeks show increased caspase 3 activity
brenda
-
upper part, expression of caspase-3 is associated with the pathologic stage in urothelial carcinomas, immunohistochemic analysis, overview
brenda
additional information
-
insulinoma cell, treatment with islet-specific cytokine pancreatic derived factor results in elevated enzyme levels which abrogates expression of cyclin-dependent kinase inhibitor 1A
brenda
-
insulinoma cell, treatment with islet-specific cytokine pancreatic derived factor results in elevated enzyme levels which abrogates expression of cyclin-dependent kinase inhibitor 1A
-
brenda
-
geldanamycin inhibits hemorrhage-induced increases in caspase-3 activity
brenda
-
senescence-accelerated prone mice 8 and senescence-accelerated resistant mice 1 show a drop in age-related proteolytic activity of caspase-3, overview
brenda
-
caspase-3 is increased in ischemic brain, in penumbra and core
brenda
-
priary neuronal cell culture derived from cerebral cortex of fetal rats
brenda
-
induction of apoptosis with mitomycin-c in presence or absence of general caspase inhibitor benzoyl-Val-Ala-Asp-fluoromethylketone. Benzoyl-Val-Ala-Asp-fluoromethylketone prevents mitomycin-c-induced cell death. In contrast, specific inhibition of enzyme or caspase-7 in presence of mitomycin-c induces necrotic-like or paraptotic-like morphological changes but does not prevent cell death
brenda
-
caspase-3 activity is significantly higher in slow developing embryos in comparison with fast cleavers, but is not related to embryo morphology. Caspase activity is significantly higher in embryos derived from growing oocytes compared with those of fully grown oocytes at 45, 80, and 117 hours post-insemination
brenda
-
present in early embryos up to the 1000-cell stage as a maternal factor, and is then expressed throughout the body after the gastrula stage by zygotic expression
brenda
-
active cleaved caspase-3 in epithelial cells of the intestine, quantitative immunohistochemical staining, overview
brenda
-
geldanamycin inhibits hemorrhage-induced increases in caspase-3 activity
brenda
-
no differences between caspase 3 activities in the hearts from mice without infarcts and caspase 3 activities in hearts from mice with infarction or ischemia
brenda
-
no differences between caspase 3 activities in the hearts from mice without infarcts and caspase 3 activities in hearts from mice with infarction or ischemia
-
brenda
-
generation of enzyme from latent proenzyme dimer upon induction of apoptosis
brenda
-
geldanamycin inhibits hemorrhage-induced increases in caspase-3 activity
brenda
-
geldanamycin inhibits hemorrhage-induced increases in caspase-3 activity
brenda
-
the caspase-3 activity is about 2.4, 3.3, and 4.7fold higher in hepatitis C virus noncirrhosis, nonalcoholic fatty liver disease, and HCV cirrhosis cohorts, respectively, compared to healthy volunteers
brenda
-
geldanamycin inhibits hemorrhage-induced increases in caspase-3 activity
brenda
-
inactive 32000 Da proform of caspase-3 is basally expressed in macrophages, virus infection induces the cleavage of procaspase into the mature 17000 Da form
brenda
-
from arteriosclerotic carotid artery, presence of proapoptotic markers such as enzyme, poly(ADP-ribose) polymerase, apoptosis-inducing factor, c-Jun/AP-1, and proinflammatory markers such as macrophage migration inhibitory factor and cyclooxygenase-2. Colocalization of proapoptic markers and proinflammatory markers and oxidized low-density lipoproteins
brenda
-
expression patterns of the major caspases, CASP3, 6, 7, 8, 9, and 10, and inhibitor of apoptosis proteins, survivin, CIAP1, CIAP2, XIAP, and livin, overview
brenda
-
West Nile virus induces caspase 3 activation and apoptosis in the brains of wild-type mice. Caspase 3-dependent apoptosis contributes to the pathogenesis of lethal West Nile virus encephalitis
brenda
-
neuronal cortical cell, during glutamte-induced apoptotic cell death, glutamate induces activation of calpain, enzyme and translocation of mitochondrial apoptosis inducing factor AIF to cytosol and nuclei. These processes are inhibited/reversed by 17beta-estradiol and DELTA8,17beta-estradiol with the latter being more potent
brenda
level of caspase-3 does not change significantly in theca tissue during follicle development. Procaspase-3 level is elevated 2-fold to 5-fold in preovulatory, compared to prehierarchal follicle granulosa cells
brenda
-
during differentiation of myoblasts to myotubes, there is an obligatory, transient increase in caspase-3 activity, accompanied by a corresponding increase in proteasome activity and cleavage of Rpt2 and Rpt6
brenda
-
CD8+CD28- T lymphocytes show significantly higher levels of caspase-3 compared with their CD28+ counterparts
brenda
additional information
-
the MCF-7 human breast carcinoma cell line is caspase-3-deficient because of the deletion of exon 3 in the caspase-3 gene
brenda
additional information
ubiquitous, constitutive expression with varying expression levels from tissue to tissue, real-time PCR expression analysis
brenda
additional information
-
ubiquitous, constitutive expression with varying expression levels from tissue to tissue, real-time PCR expression analysis
brenda
additional information
-
type I cells generate high levels of caspase-3
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
bound to heavy membrane fraction, the N-termini of activated heavy-membrane-bound and cytoplasmic caspase-3 are slightly different: the heavy membrane caspase-3 begins at Lys14, whereas the cytoplasmic enzyme begins at Ser10
brenda
-
activated enzyme, the enzyme harbors one crm-1-independent nuclear export signal but no nuclear localization signal residing at the small subunit of caspase-3. The nuclear entry of active caspase-3 is not mediated by passive diffusion, but by its p3-recognition-based specific cleavage activity. The p3-mediated cleavage activity abrogates the function of the nuclear localization signal in caspase-3, which is essential for the active caspase-3 to enter into the nucleus
brenda
additional information
-
the N-termini of activated heavy-membrane-bound and cytoplasmic caspase-3 are slightly different: the heavy membrane caspase-3 begins at Lys14, whereas the cytoplasmic enzyme begins at Ser10
brenda
additional information
-
p3-mediated cleavage activity abrogates the functions of other crm-1-dependent nuclear export signals with low nuclear export signal activity
-
brenda
additional information
-
caspase-3 and its activation is not associated with TNF receptosomes. Neither caspase-3 nor cleaved caspase-3 are present in receptosomes
-
brenda
additional information
-
co-localization with Fas death domain, FADD
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
caspases-3 is a member of the cysteine-aspartic acid protease (caspase) family, fish caspase-3 subgroup. Lyccasp3 exhibits a conserved caspase-3 architecture including a prodomain, a large subunit and a small subunit. Several residues critical in the caspase-3 catalytic centre and binding pocket, as well as the active-site pentapeptide motif Q172ACRG176, are present in the deduced Lyccasp3 sequence, phylogenetic tree, overview
malfunction
-
mutations disrupting the cleavage activity or the p3 recognition site cause a defect in the nuclear entry of active caspase-3
malfunction
-
in mice with a muscle wasting condition, chronic kidney disease, occurs cleavage of subunits Rpt2 and Rpt6 and stimulation of proteasome activity
malfunction
-
caspase-3-specific inhibition augments RANKL-induced osteoclast differentiation in RAW264 cells and mouse bone marrow macrophages
metabolism
the intrinsic apoptotic pathway, which is initiated by caspase-9 and executed by caspase-3, is activated during the immune response induced by poly(I:C) or bacterial vaccine in the fish
metabolism
-
the stage of muscle cell differentiation determines not only the caspase-3-induced subunit cleavage patterns but also the changes in proteasome activity
metabolism
-
tumour necrosis factor, TNF, induced ceramide production by endosomal acid sphingomyelinase, A-SMase, couples to apoptosis signalling via activation of cathepsin D and cleavage of Bid, resulting in caspase-9 and caspase-3 activation
physiological function
-
caspase-3 exists in the form of pro-enzyme, and is located predominantly in the cytoplasm of cells. During apoptosis, caspase-3 is cleaved and activated by upstream caspases, and is translocated into the nucleus to cleave its nuclear substrates, resulting in characteristic apoptotic nuclear changes such as DNA fragmentation, chromatin condensation and nuclear disruption
physiological function
-
caspase-3 cleaves specific 19 S proteasome subunits in skeletal muscle stimulating proteasome activity. Caspase-3 increases proteasome activity in myotubes but not in myoblasts by cleaving Rpt2 and Rpt6, while in myoblasts, caspase-3 cleaves Rpt5 to decrease proteasome activity, a feed-forward amplification that augments muscle proteolysis in catabolic conditions, overview
physiological function
-
caspase-3 activates acid sphingomyelinase, i.e. A-SMase, but pro-A-SMase is not a direct substrate for caspase-3
physiological function
-
caspase 8 is an initiator caspase for caspase 3 during H2O2-induced apoptosis. During H2O2-induced apoptosis, caspase 3 is activated directly through caspase 8 and not through the mitochondriadependent caspase 9 activation
physiological function
-
the enzyme can exert a caspase executer function during potato-Phytophthora infestans interaction, resulting in the restriction of the pathogen spread during plant-pathogen interaction
physiological function
-
caspase-3 is involved in normal protein turnover caused by, for example, incident light
physiological function
-
activation of caspase-3 plays an inhibitory role at the late stage of RANKL-induced osteoclast differentiation
physiological function
compensatory growth and regeneration of skeletal muscle is dependent on the resident stem cell population, satellite cells (SCs). Self-renewal and maintenance of the SC niche is coordinated by the paired-box transcription factor Pax7. Continued expression of this protein inhibits the myoblast differentiation program. Caspase 3 cleavage inactivation of Pax7 is a crucial step for terminating the self-renewal process
physiological function
cleavage by caspase-3 is a crucial upstream event associated with Tau self-assembly leading to Alzheimer's Disease pathogenesis
physiological function
caspase-3 serves as an intracellular immune receptor specific for lipopolysaccharide. The interaction of lipopolysaccharide with CgCaspase-3 specifically inhibits the cell apoptosis induced by CgCaspase-3
additional information
-
tichothecin induces apoptosis of HepG2 cells via caspase-9 mediated activation of the mitochondrial death pathway. Trichothecin increases caspase-9 expression and caspase-3 activity
additional information
-
active caspase-3 does not colocalize with internalized TNF-R1 receptosomes
Show AA Sequence and Transmembrane Helices (1391 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13000
-
x * 33000, precursor form, x * 29000, mature form processed at prodomain alone, i.e. large subunit, x * 13000, small subunit, SDS-PAGE
15000
-
x * 15000, recombinant, active processed enzyme, SDS-PAGE, x * 35000, recombinant, inactive unprocessed enzyme, SDS-PAGE
29000
-
x * 33000, precursor form, x * 29000, mature form processed at prodomain alone, i.e. large subunit, x * 13000, small subunit, SDS-PAGE
33000
-
x * 33000, precursor form, x * 29000, mature form processed at prodomain alone, i.e. large subunit, x * 13000, small subunit, SDS-PAGE
35000
-
x * 15000, recombinant, active processed enzyme, SDS-PAGE, x * 35000, recombinant, inactive unprocessed enzyme, SDS-PAGE
additional information
additional information
full-length proCPP32 has a molecular weight of 32000-33000 Da
additional information
-
full-length proCPP32 has a molecular weight of 32000-33000 Da
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
active caspase-3 is a homodimer of two heterodimer subunits, with one active site on each subunit
additional information
?
-
x * 33000, precursor form, x * 29000, mature form processed at prodomain alone, i.e. large subunit, x * 13000, small subunit, SDS-PAGE
?
-
x * 15000, recombinant, active processed enzyme, SDS-PAGE, x * 35000, recombinant, inactive unprocessed enzyme, SDS-PAGE
additional information
-
two bands of 12000 Da and 17000 Da are detected by SDS-PAGE
additional information
-
caspase-3 is expressed as an inactive 32 kDa precursor from which the p20 and p11 subunits are proteolytically generated during onset of apoptosis
additional information
Lyccasp3 exhibits a conserved caspase-3 architecture including a prodomain, a large subunit and a small subunit
additional information
-
Lyccasp3 exhibits a conserved caspase-3 architecture including a prodomain, a large subunit and a small subunit
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
additional information
-
caspase-3 is S-nitrosylated under basal conditions to prevent activation
proteolytic modification
-
different processsing of membrane-bound and cytoplasmic enzyme
proteolytic modification
both Mch4 and granzyme B cleave recombinant proCPP32 at a conserved IXXD-S sequence to produce the large and small subunits of the active protease. Granzyme B cleaves at Asp175 to generate the small C-terminal subunit, 12000 Da, and te large N-terminal subunit. Cleavage of the prodomain is an autocatalytic activity of the activated CPP32
proteolytic modification
-
inactive 32000 Da proform of caspase-3 is basally expressed in macrophages, virus infection induces the cleavage of procaspase into the mature 17000 Da form
proteolytic modification
-
pro-caspase-3 is cleaved and activated to caspase-3, pre-treatment of cells with HA14-1 followed by paclitaxel induces cleavage of pro-caspase-3 to active form
proteolytic modification
-
caspases are synthesized in the cell as single-chain precursors and are activated by cleavage at the conserved Asp297 residue, where a conformational change occurs bringing it into the correct alignment for catalysis
proteolytic modification
-
during spontaneous neutrophil apoptosis caspase-3 are rapidly activated
proteolytic modification
-
caspase-3 is expressed as an inactive 32 kDa precursor from which the p20 and p11 subunits are proteolytically generated during onset of apoptosis
proteolytic modification
-
caspase-8 is activated when procaspase-8 is cleaved subsequently from the recruitment of Fas associated protein with death domain, FADD, to the death-effector domain site of procaspase-8 during the oligomerization of death receptor and its ligand
proteolytic modification
-
caspase-9 and caspase-8 activate procaspase-3 to caspase-3 by cleavage
proteolytic modification
-
procaspase-8 is cleaved to 41 and 43 kDA fragments, overview
proteolytic modification
-
upon purification and activation, caspase-3 subunits A and B are processed to yield the sequences S29GIS...IETD175 and S176GVD
YFYH277-(H)7
proteolytic modification
-
cleavage of procaspase-3 to the active 17 kDa form. Caspase-3 activation occurs after TNF stimulation at later time points and is not associated with TNF receptosomes
proteolytic modification
-
caspase-9 and caspase-8 activate procaspase-3 to caspase-3 by cleavage
proteolytic modification
-
caspase-3 is activated from procaspase-3 by cleavage
proteolytic modification
-
procaspase-3 is activated by cleavage through caspase-8 and caspase-9 leading to apoptosis
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
caspase-3 in complex with beta-strand urazole ring-containing irreversible peptidomimetic inhibitor compound-1, vapor diffusion, at 4°C, from 0.005 ml drops containing equal volumes of 16% ethanol, 0.1 M Tris buffer, pH 7.8, and the protein complex solution, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement
-
co-crystals of the complex between recombinant human caspase-3 and azapeptide epoxide inhibitors are grown from hanging drops
-
complex of caspase-3 with (S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid and (S)-5-[[5-[1-carboxylmethyl-3-(2-chlorobenzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid, hanging drop vapor diffusion method
-
crystal structure of recombinant enzyme in complex with acetyl-Asp-Val-Ala-Asp fluoromethyl ketone, hanging and sitting drop vapor diffusion method
-
in complex with inhibitors acetyl-Asp-Glu-Val-Asp-aldehyde, acetyl-Val-Asp-Val-Ala-Asp-aldehyde, acetyl-Asp-Met-Gln-Asp-aldehyde
recombinant enzyme in complex with inhibitors Ac-IEPD-Cho, Ac-WEHD-Cho, Ac-YVADCho, and Boc-D(OMe)-fluoromethyl ketone, caspase-3 is incubated at room temperature with the inhibitor at 10 to 20fold molar excess, followed by crystallization via the hanging-drop vapor diffusion method, 0.001 ml of 4 mg/ml protein in solution is mixed with an equal volume of mother liquid containing 100 mM sodium citrate, 5% glycerol, 10 mM DTT, and 14-18% PEG 6000, pH 6.5, 24 h at room temperature, X-ray diffraction structure determination and analysis at 1.9-2.6 A resolution, molecular replacement, modelling, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C143A
-
inactive enzyme. Catalytically inactive p17 polypeptide is expressed in a stable manner, while wild-type p17 is rapidly degraded
D179A
increase both in kcat- and KM-value. D179 is involved in substrate recognition
R64E
-
site-directed mutagenesis, the mutant existed in the nuclear fraction, the subcellular localization signal in the rev-caspase-3 is not disrupted by the R64E mutation
C163G
-
transfection of human breast cancer cells lacking enzyme with wild-type or mutant cDNA. Expression of wild-type, but not the inactive mutants C163G or C163S, is associated with increased enzyme activity and susceptibility to staurosporine-induced apoptosis. Wild-type and mutant transfection results in inhibition of cell growth and decrease in phosphorylation of the Akt protein compared to control
C163S
-
transfection of human breast cancer cells lacking enzyme with wild-type or mutant cDNA. Expression of wild-type, but not the inactive mutants C163G or C163S, is associated with increased enzyme activity and susceptibility to staurosporine-induced apoptosis. Wild-type and mutant transfection results in inhibition of cell growth and decrease in phosphorylation of the Akt protein compared to control
additional information
additional information
-
engineering of CHO cells for more robust cell lines includes reduction of apoptotic capase-3, activities in different mutant cell lines, overview. The cells exhibit a reduction in caspase 3 activity of at least 60% and a 170% enhancement in mitochondrial membrane potential compared to controls when treated with staurosporine
additional information
-
caspase-3 gene silencing leads to inhibition of apoptosis in insulinoma cells and human islets, caspase-3 upregulation leads to the generation of active caspase-6 and caspase-7, which in turn degrade a number of intracellular protein substrates
additional information
-
construction of an in vivo mouse hind limb H460 lung cancer model
additional information
caspase-3 knockout by shRNA, generation of double knockdown cells lacking caspase-3 and caspase-7, EC 3.4.22.60, activity. Generation of caspase-7-based chimeric constructs with various regions of caspase-3, EC 3.4.22.56
additional information
-
caspase-3 knockout by shRNA, generation of double knockdown cells lacking caspase-3 and caspase-7, EC 3.4.22.60, activity. Generation of caspase-7-based chimeric constructs with various regions of caspase-3, EC 3.4.22.56
additional information
engineering of a light-activated human caspase-3 (Caspase-LOV) by exploiting its natural spring-loaded activation mechanism through rational insertion of the light-sensitive LOV2 domain that expands upon illumination
additional information
-
engineering of a light-activated human caspase-3 (Caspase-LOV) by exploiting its natural spring-loaded activation mechanism through rational insertion of the light-sensitive LOV2 domain that expands upon illumination
additional information
-
construction of a caspase-3/-7 double-knockout mouse embryonic fibroblasts cell model for studying of autophagy contributing to the mechanism of increased cell death, following inhibition of apoptosis
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by nickel affinity chromatography, ion exchange chromatography, and gel filtration
recombinant His6-tagged caspase-3 from Escherichia coli by nickel affinity chromatography
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upon purification and activation, caspase-3 subunits A and B are processed to yield the sequences S29GIS...IETD175 and S176GVD
YFYH277-(H)7, the purified enzyme shows 90% of maximum activity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
caspase-3 expression analysis
cloning of full-length cDNA of Lyccasp3, DNA and amino acid sequence determination and analysis, phylogenetic tree, real-time PCR expression analysis, functional recombinant expression in Escherichia coli strain BL21 (DE3)
engineering of a light-activated human caspase-3 (Caspase-LOV) by exploiting its natural spring-loaded activation mechanism through rational insertion of the light-sensitive LOV2 domain that expands upon illumination. Using the tissue-specific expression system (UAS)-GAL4, Caspase-LOV is specifically expressed in three neuronal cell types: retinal, sensory, and motor neuron of Drosophila
expression in Escherichia coli
expression of FLAG-tagged caspase-3 in DKD cells. Simultaneous expression of HA-procaspase-3 and HA-procaspase-7, EC 3.4.22.60, in DKD HeLa cells together with FLAG-caspase-3 or FLAG-caspase-7. HA-procaspase-3 is coimmunoprecipitated with FLAG-procaspase-3 but not with FLAG-procaspase-7. Similarly, HA-procaspase-7 is co-immunoprecipitated with FLAG-procaspase-7 but not with FLAG-procaspase-3
expression of His6-tagged caspase-3 in Escherichia coli, effects of transiently-expressed VhhCasp31 and VhhCasp32 intrabodies on oxidative-stress-induced apoptosis in SHSY-5Y cells, overview
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GFP-tagged subunit and enzyme expression, the small subunit as well as the full-length caspase-3 display evident cytoplasm localization, while the large subunit and its truncated forms are distributed throughout the whole cell
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quantitative expression analysis in several ovarian and endometrial cancer cell lines by RT-PCR
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sequence encoding the caspase-3 catalytic domain (no prodomain) with a C-terminal hexa-His tag is inserted into vector pET-16b and expressed in Escherichia coli BL21
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the full-length caspase-3 gene containing an N-terminal 6His-tag is expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
administration of ethanol induces a transient increase of the expression of caspase-3 which can be partially blocked by the pituitary adenylate cyclase-activating polypeptide
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astaxanthine at 0.1 mM protects PC12 cells from damaging effects of beta-amyloid peptide 25-35 by partially down-regulating the activation of caspase 3
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caspase-3 activity in gastric mucosa shows 2.5fold increase in non-diabetic rats that receive indomethacin, 3.5fold increase in diabetic indomethacin-treated rats, and 1fold-increase in diabetic telmisartan-treated rats that receive indomethacin as compared to the control group
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caspase-3 levels are significantly elevated in the diabetic rat sciatic nerve
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cooperative apoptosis induction by melatonin and doxorubicin is associated with increased expression of caspase 3
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crude Silybum marianum extract treatments significantly lower activation of procaspase-3 to active caspase-3
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following prolonged epileptic seizures, a mild as well as a severe insult produces caspase-3-negative necrotic neurons
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in contrast to low XIAP expression, the A5-16 strain shows enhanced cleavage of caspase-3 as early as 8 hours post infection with a 6-8fold increase by 12 hours post infection. There is a significant increase in caspase-3 activity (2-3fold) at an early stage of infection (4-8 hours post infection) in mutant strain A5-16-infected cells compared to the A5-13 infection. At 12-18 hours post infection, the caspase-3 activity in A5-13-infected cells increases significantly relative to mock-infected controls
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quick induction fo expression in spleen and kidney by stimulation with either poly(I:C) or inactivated trivalent bacterial vaccine
serum caspase-3 decreases 5.8 times in rats with human umbilical cord mesenchymal stem cells transplantated via the left carotid artery compared to control groups
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sesamol treatment significantly and dose-dependently inhibits caspase-3 activity in streptozotocin-injected rats
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significant correlation is seen between plasma nitrite/nitrate-concentrations and caspase-3 activity, which is significantly higher in patients with schizophrenia than in controls
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there is an about 4fold increase of activated caspase-3 expression 4 days after high dose treatment with 100 nM L-arginase in Panc-1 and Hep-3B cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
drug development
medicine
molecular biology
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engineering of CHO cells for more robust cell lines includes reduction of apoptotic capase-3, overview
analysis
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cell-permeable substrate N-acetyl-L-Asp-L-Glu-L-Val-L-Asp-N-morpholinecarbonyl-rhodamine 110, high turnover rate and sensitivity both in enzyme solution and in living cells
analysis
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the highly cell-permeable caspase-3 substrate is obtained by linking a fluorogenic DNA-binding dye to the caspase-3 recognition sequence that renders the dye nonfunctional. On substrate cleavage, the dye is released and becomes highly fluorescent on binding to DNA. DEVD-NucView488 detects caspase-3 activation within a live-cell population much earlier and with higher sensitivity compared with other apoptosis reagents. Cells incubated with DEVD-NucView488 exhibit no toxicity and normal apoptotic progression. DEVD-NucView488 is an ideal substrate for kinetic studies of caspase-3 activation because it detects caspase-3 activity in real-time and also efficiently labels DNA in nuclei of caspase-3-activated cells for real-time fluorescent visualization of apoptotic morphology
diagnostics
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a simple biochemical assay of caspase-3 activity in blood, may be useful for predicting the disposition of drugs that undergo extensive conjugation and biliary elimination like silymarin in patients with liver disease, caspase-3 activity correlates with the amount of silymarin conjugates, e.g. silychristin and silybin A and B, and is 5fold higher in the HCV cirrhosis cohort, overview
diagnostics
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caspase-3 is a helpful indicator of apoptosis induction, e.g. in mammary carcinomas
diagnostics
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caspase-3 activity is a marker for apoptosis in gut epithelium, leading to impairment of the gastrointestinal mucosal barrier, that contributes to progression of HIV infection, immunohistochemical staining of cleaved caspase-3, overview
diagnostics
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caspase-3 is a marker for apoptosis, e.g. useful in patients with urothelial carcinoma of the upper urinary tract, overview
diagnostics
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caspase-3 is a marker of apoptotic cell death in embryonic fibroblasts, NIH-3T3 and WST-1 cells
diagnostics
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caspase-3 activity is a marker for cell death, e.g. in microglia, overview
diagnostics
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active caspase-3 immunostaining is considered as a highly reliable and specific morphological marker of early apoptosis
drug development
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the VHH proteins, isolated from heavy chain antibody variable domain, i.e. VHH phage display library, are antagonist and agonist of apoptosis and could have potential for the development of therapeutics for neurodegenerative diseases and cancer, respectively
drug development
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caspase-3 ia a target for structure-based drug design approach
medicine
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PANDER-induced downregulation of cyclin-dependent kinase inhibitor 1A expression coupled with induced CASP3-activation may serve a central role in islet cell death and offers further insight into the mechanisms of cytokine-induced beta-cell apoptosis
medicine
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induction of apoptosis with mitomycin-c in presence or absence of general caspase inhibitor benzoyl-Val-Ala-Asp-fluoromethylketone. Benzoyl-Val-Ala-Asp-fluoromethylketone prevents mitomycin-c-induced cell death. In contrast, specific inhibition of enzyme or caspase-7 in presence of mitomycin-c induces necrotic-like or paraptotic-like morphological changes but does not prevent cell death
medicine
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during glutamte-induced apoptotic cell death, glutamate induces activation of calpain, enzyme and translocation of mitochondrial apoptosis inducing factor AIF to cytosol and nuclei. These processes are inhibited/reversed by 17beta-estradiol and DELTA8,17beta-estradiol with the latter being more potent
medicine
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during glutamte-induced apoptotic cell death, at least two mechanisms are involved: a caspase-3-dependent pathway and an enzyme-independent pathway using calpain and apoptosis inducing factor
medicine
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in macrophages from arteriosclerotic carotid artery, presence of proapoptotic markers such as enzyme, poly(ADP-ribose) polymerase, apoptosis-inducing factor, c-Jun/AP-1, and proinflammatory markers such as macrophage migration inhibitory factor and cyclooxygenase-2. Colocalization of proapoptic markers and proinflammatory markers and oxidized low-density lipoproteins
medicine
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caspase 3-dependent apoptosis contributes to the pathogenesis of lethal West Nile virus encephalitis and suggests possible novel therapeutic targets to restrict injury of central nervous system
medicine
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geldanamycin limits caspase-3 expression and protects from organ injury by suppressing inducible nitric oxide synthase expression and apoptosome formation. Geldanamycin, therefore may prove useful as an adjuvant in fluids used to treat patients suffering blood loss
medicine
light-activated caspase-3 can be used for precise ablation of neurons in vivo
medicine
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PANDER-induced downregulation of cyclin-dependent kinase inhibitor 1A expression coupled with induced CASP3-activation may serve a central role in islet cell death and offers further insight into the mechanisms of cytokine-induced beta-cell apoptosis
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EXTERNAL LINKS (specific for EC-Number 3.4.22.56)
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Release 2026.1 (March 2026)
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