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Information on EC 3.4.22.56 - caspase-3 and Organism(s) Rattus norvegicus and UniProt Accession P55213

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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
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Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P55213 not found.
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
strict requirement for an Asp residue at 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
apopain
-
-
-
-
C14.003
-
-
-
-
CASP-3
-
-
-
-
caspase 3
CPP-32
-
-
-
-
CPP32
-
-
-
-
CPP32/apopain
-
-
-
-
cysteine protease CPP32
-
-
-
-
IRP
-
-
-
-
SCA-1
-
-
-
-
SREBP cleavage activity 1
-
-
-
-
Yama protein
-
-
-
-
Yama/CPP32
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
169592-56-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-DEVD-4-nitroanilide + H2O
Ac-DEVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
show the reaction diagram
-
the active site of caspase-3 is located at Cys163, which plays a key role in substrate hydration
-
-
?
Asp-Glu-Val-Asp-4-nitroanilide + H2O
Asp-Glu-Val-Asp + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Bid peptide + H2O
?
show the reaction diagram
-
-
-
-
?
DEVD-4-nitroanilide + H2O
DEVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
DEVD-7-amido-4-fluoromethylcoumarin + H2O
DEVD + 7-amino-4-fluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
IETD-4-nitroanilide + H2O
IETD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
procaspase-3 + H2O
caspase-3 + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Bid peptide + H2O
?
show the reaction diagram
-
-
-
-
?
procaspase-3 + H2O
caspase-3 + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-hydroxyl-anthranilamide
-
inhibits caspase-3, the compound is isolated from Streptomyces sp., a mangrove actinomycete, strain 061316
8-hydroxyl-2,4-dioxoquinazoline
-
inhibits caspase-3, the compound is isolated from Streptomyces sp., a mangrove actinomycete, strain 061316
Asp-Glu-Val-Asp-fluoromethylketone
-
-
benzyloxycarbonyl-VAD-fluoromethylketone
-
-
bradykinin
-
prevents caspase-3 activation in neurons
HBx
-
hepatitis virus Hbx protein, potent
-
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-benzyloxycarbonyl-valyl-alanyl-aspartic-acid fluoromethyl ketone
-
-
N-carbobenzyloxy-DEVD-fluoromethyl ketone
-
a specific caspase-3 inhibitor
survivin
-
inhibits processing of procaspase-3 and specifically binds the active form of caspase-3 through a baculovirus inhibitor of apoptosis, IAP, repeat domain
-
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
Val-Ala-Asp-fluoromethylketone
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
carboxyfluorescein-valyl-alanyl-aspartic-acid fluoromethyl ketone
-
the FAM-peptide irreversibly binds to active caspases
cytochrome c
-
forebrain ischemia causes release of cytochrome c from mitochondria and translocation to the nucleus, which induces caspase-3 activation
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
-
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032
3-hydroxyl-anthranilamide
Rattus norvegicus
-
pH 7.5, 35°C
0.036
8-hydroxyl-2,4-dioxoquinazoline
Rattus norvegicus
-
pH 7.5, 35°C
0.0102
myricetin
Rattus norvegicus
-
pH 7.4, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
retinal
Manually annotated by BRENDA team
-
the active caspase-3 expression is higher in the anterior pole of the lens
Manually annotated by BRENDA team
-
inguinal lymph node, ILN cell
Manually annotated by BRENDA team
-
gastric mucosal cell
Manually annotated by BRENDA team
-
constitutive caspase-3 activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
co-localization with Fas death domain, FADD
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
caspase-3 is involved in normal protein turnover caused by, for example, incident light
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CASP3_RAT
277
0
31492
Swiss-Prot
other Location (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
caspase-3 expression analysis
-
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
-
amifostine increases caspase-3 expression
-
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
-
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
-
caspase-3 levels are significantly elevated in the diabetic rat sciatic nerve
-
crude Silybum marianum extract treatments significantly lower activation of procaspase-3 to active caspase-3
-
following prolonged epileptic seizures, a mild as well as a severe insult produces caspase-3-negative necrotic neurons
-
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
-
sesamol treatment significantly and dose-dependently inhibits caspase-3 activity in streptozotocin-injected rats
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Flaws, J.A.; Kugu, K.; Trbovich, A.M.; Desanti, A.; Tilly, K.I.; Hirshfield, A.N.; Tilly, J.L.
Interleukin-1 beta-converting enzyme-related proteases (IRPs) and mammalian cell death: dissociation of IRP-induced oligonucleosomal endonuclease activity from morphological apoptosis in granulosa cells of the ovarian follicle
Endocrinology
136
5042-5053
1995
Rattus norvegicus (P55213)
Manually annotated by BRENDA team
Ni, B.; Wu, X.; Du, Y.; Su, Y.; Hamilton-Byrd, E.; Rockey, P.K.; Rosteck, P.Jr.; Poirier, G.G.; Paul, S.M.
Cloning and expression of a rat brain interleukin-1beta-converting enzyme (ICE)-related protease (IRP) and its possible role in apoptosis of cultured cerebellar granule neurons
J. Neurosci.
17
1561-1569
1997
Rattus norvegicus (P55213)
Manually annotated by BRENDA team
Gottlob, K.; Fulco, M.; Levrero, M.; Graessmann, A.
The hepatitis B virus HBx protein inhibits caspase 3 activity
J. Biol. Chem.
273
33347-33353
1998
Rattus norvegicus
Manually annotated by BRENDA team
Zhang, Y.; Bhavnani, B.R.
Glutamate-induced apoptosis in neuronal cells is mediated via caspase-dependent and independent mechanisms involving calpain and caspase-3 proteases as well as apoptosis inducing factor (AIF) and this process is inhibited by equine estrogens
BMC Neurosci.
7
49
2006
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Faraglia, B.; Bonsignore, A.; Scaldaferri, F.; Boninsegna, A.; Cittadini, A.; Mancuso, C.; Sgambato, A.
Caspase-3 inhibits the growth of breast cancer cells independent of protease activity
J. Cell. Physiol.
202
478-482
2005
Rattus norvegicus
Manually annotated by BRENDA team
Goebel, D.J.
Selective blockade of CaMKII-alpha inhibits NMDA-induced caspase-3-dependent cell death but does not arrest PARP-1 activation or loss of plasma membrane selectivity in rat retinal neurons
Brain Res.
1256
190-204
2009
Rattus norvegicus
Manually annotated by BRENDA team
Jiang, W.; Zhu, Z.; Thompson, H.J.
Effects of physical activity and restricted energy intake on chemically induced mammary carcinogenesis
Cancer Prev. Res. (Phila.)
2
338-344
2009
Rattus norvegicus
Manually annotated by BRENDA team
Danielisova, V.; Gottlieb, M.; Nemethova, M.; Krav?ukova, P.; Domorakova, I.; Mechirova, E.; Burda, J.
Bradykinin postconditioning protects pyramidal CA1 neurons against delayed neuronal death in rat hippocampus
Cell. Mol. Neurobiol.
29
871-878
2009
Rattus norvegicus
Manually annotated by BRENDA team
Mustonen, H.; Puolakkainen, P.; Kemppainen, E.; Kiviluoto, T.; Kivilaakso, E.
Taurocholate potentiates ethanol-induced NF-kappaB activation and inhibits caspase-3 activity in cultured rat gastric mucosal cells
Digest. Dis. Sci.
54
928-936
2009
Rattus norvegicus
Manually annotated by BRENDA team
Kalm, M.; Lannering, B.; Bjoerk-Eriksson, T.; Blomgren, K.
Irradiation-induced loss of microglia in the young brain
J. Neuroimmunol.
206
70-75
2009
Rattus norvegicus
Manually annotated by BRENDA team
Shimmyo, Y.; Kihara, T.; Akaike, A.; Niidome, T.; Sugimoto, H.
Three distinct neuroprotective functions of myricetin against glutamate-induced neuronal cell death: involvement of direct inhibition of caspase-3
J. Neurosci. Res.
86
1836-1845
2008
Rattus norvegicus
Manually annotated by BRENDA team
Camelo, S.; Lajavardi, L.; Bochot, A.; Goldenberg, B.; Naud, M.C.; Brunel, N.; Lescure, B.; Klein, C.; Fattal, E.; Behar-Cohen, F.; de Kozak, Y.
Protective effect of intravitreal injection of vasoactive intestinal peptide-loaded liposomes on experimental autoimmune uveoretinitis
J. Ocul. Pharmacol. Ther.
25
9-21
2009
Rattus norvegicus
Manually annotated by BRENDA team
Amantini, C.; Mosca, M.; Lucciarini, R.; Perfumi, M.C.; Santoni, G.
Thiorphan-induced survival and proliferation of rat thymocytes by activation of Akt/survivin pathway and inhibition of caspase-3 activity
J. Pharmacol. Exp. Ther.
327
215-225
2008
Rattus norvegicus
Manually annotated by BRENDA team
Sun, M.; Zhao, Y.; Gu, Y.; Xu, C.
Inhibition of nNOS reduces ischemic cell death through down-regulating calpain and caspase-3 after experimental stroke
Neurochem. Int.
54
339-346
2009
Rattus norvegicus
Manually annotated by BRENDA team
Guerleyen, H.; Christiansen, H.; Tello, K.; Dudas, J.; Hermann, R.M.; Rave-Fraenk, M.; Hess, C.F.; Ramadori, G.; Saile, B.
Irradiation leads to sensitization of hepatocytes to TNF-alpha-mediated apoptosis by upregulation of IkappaB expression
Radiat. Environ. Biophys.
48
85-94
2009
Rattus norvegicus
Manually annotated by BRENDA team
Teschendorf, P.; Vogel, P.; Wippel, A.; Krumnikl, J.J.; Spoehr, F.; Boettiger, B.W.; Popp, E.
The effect of intracerebroventricular application of the caspase-3 inhibitor zDEVD-FMK on neurological outcome and neuronal cell death after global cerebral ischaemia due to cardiac arrest in rats
Resuscitation
78
85-91
2008
Rattus norvegicus
Manually annotated by BRENDA team
Cao, H.; Qian, H.; Xu, W.; Zhu, W.; Zhang, X.; Chen, Y.; Wang, M.; Yan, Y.; Xie, Y.
Mesenchymal stem cells derived from human umbilical cord ameliorate ischemia/reperfusion-induced acute renal failure in rats
Biotechnol. Lett.
32
725-732
2010
Rattus norvegicus
Manually annotated by BRENDA team
Fouad, A.A.; Al-Sultan, A.I.; Yacoubi, M.T.; Gomaa, W.
Ameliorative effects of telmisartan in diabetic rats with indomethacin-induced gastric ulceration
Eur. J. Pharmacol.
637
162-170
2010
Rattus norvegicus
Manually annotated by BRENDA team
Aghazadeh, S.; Amini, R.; Yazdanparast, R.; Ghaffari, S.H.
Anti-apoptotic and anti-inflammatory effects of Silybum marianum in treatment of experimental steatohepatitis
Exp. Toxicol. Pathol.
63
569-574
2011
Rattus norvegicus
Manually annotated by BRENDA team
Chang, C.H.; Chen, C.Y.; Chiou, J.Y.; Peng, R.Y.; Peng, C.H.
Astaxanthine secured apoptotic death of PC12 cells induced by beta-amyloid peptide 25-35: its molecular action targets
J. Med. Food
13
548-556
2010
Rattus norvegicus
Manually annotated by BRENDA team
Chopra, K.; Tiwari, V.; Arora, V.; Kuhad, A.
Sesamol suppresses neuro-inflammatory cascade in experimental model of diabetic neuropathy
J. Pain
11
950-957
2010
Rattus norvegicus
Manually annotated by BRENDA team
Chok, M.K.; Conti, M.; Almolki, A.; Ferlicot, S.; Loric, S.; Duerrbach, A.; Benoit, G.; Droupy, S.; Eschwege, P.
Renoprotective potency of amifostine in rat renal ischaemia-reperfusion
Nephrol. Dial. Transplant.
25
3845-3851
2010
Rattus norvegicus
Manually annotated by BRENDA team
Fujikawa, D.G.; Zhao, S.; Ke, X.; Shinmei, S.S.; Allen, S.G.
Mild as well as severe insults produce necrotic, not apoptotic, cells: evidence from 60-min seizures
Neurosci. Lett.
469
333-337
2010
Rattus norvegicus
Manually annotated by BRENDA team
Botia, B.; Jolivel, V.; Burel, D.; Le Joncour, V.; Roy, V.; Naassila, M.; Benard, M.; Fournier, A.; Vaudry, H.; Vaudry, D.
Neuroprotective Effects of PACAP Against Ethanol-Induced Toxicity in the Developing Rat Cerebellum
Neurotox. Res.
19
423-434
2010
Rattus norvegicus
Manually annotated by BRENDA team
Chen, G.; Gao, H.; Tang, J.; Huang, Y.; Chen, Y.; Wang, Y.; Zhao, H.; Lin, H.; Xie, Q.; Hong, K.; Li, J.; Yao, X.
Benzamides and quinazolines from a mangrove actinomycetes Streptomyces sp. (No. 061316) and their inhibiting caspase-3 catalytic activity in vitro
Chem. Pharm. Bull.
59
447-451
2011
Rattus norvegicus
Manually annotated by BRENDA team
Talebizadeh, N.; Yu, Z.; Kronschlaeger, M.; Hallboeoek, F.; Soederberg, P.
Specific spatial distribution of caspase-3 in normal lenses
Acta Ophthalmol.
93
289-292
2015
Rattus norvegicus
Manually annotated by BRENDA team