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Information on EC 3.4.22.52 - calpain-1
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3.4.22.52 calpain-1Specify your search results
Word Map
- 3.4.22.52
- calpains
- calpastatin
-
ca2+-dependent
-
tender
-
calcium-dependent
-
meat
- cytoskeletal
- beef
- ischemia
- myofibrillar
- hippocampal
- calpeptin
-
autolysis
-
caspase
- proteinase
- spectrin
- longissimus
-
calpain-mediated
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postmortem
- cathepsins
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calpain-specific
- leupeptin
- lumborum
- medicine
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sarcomere
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non-lysosomal
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nebulin
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calpain-dependent
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slaughter
-
calpain-like
- semimembranosus
- fodrin
- food industry
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carcass
-
angus
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autoproteolysis
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warner-bratzler
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autolyzed
-
ca2+-activated
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steak
- caspase-12
- myofibril
- talin
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troponin-t
-
brahman
-
calmodulin-like
- thoracis
-
proteolyzed
- aif
-
canps
- alpha-spectrin
- desmin
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mu-calpain, calpain-1, calpain i, capn1, calpain 1, capn2, micro-calpain, capns1, calpain1, calpain-i, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
calcium-activated neutral protease I
-
-
-
-
calpain 1
calpain 1-gamma
calpain I
calpain-1
calpain-I
calpain1
CAPN1
CAPN1 g.p. (Homo sapiens)
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-
-
-
EC 3.4.24.5
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-
formerly, part transferred
-
micro-calpain
mu-calpain
muCANP
-
-
-
-
calpain 1
-
-
-
-
calpain 1
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-
calpain 1
-
-
calpain I
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-
-
-
micro-calpain
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-
-
-
mu-calpain
-
-
-
-
mu-calpain
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
broad endopeptidase specificity
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
endopeptidase
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hydrolysis of peptide bond
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peptides, endopeptidase
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CAS REGISTRY NUMBER
COMMENTARY
689772-75-6
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78990-62-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4-(4-dimethylaminophenylazo)benzoyl)-TPLKSPPPSPR-(5[(2-aminoethyl)amino]naphthalene-1-sulfonic acid) + H2O
(4-(4-dimethylaminophenylazo)benzoyl)-TPLK + SPPPSPR-(5[(2-aminoethyl)amino]naphthalene-1-sulfonic acid)
-
-
-
-
?
(5(6)-carboxyfluorescin)-GGGQLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-RRK-(5- and 6-carboxytetramethylrhodamine)-OH + H2O
(5(6)-carboxyfluorescin)-GGGQLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-RRK-(5- and 6-carboxytetramethylrhodamine)-OH
-
-
-
-
?
(EDANS)-EALFAERK-(DABCYL) + H2O
(EDANS)-EA + LFAERK-(DABCYL)
-
about 30% cleavage preference
-
-
?
(EDANS)-EPLFAARK-(DABCYL) + H2O
(EDANS)-EPLFA + ARK-(DABCYL)
-
the sequence PLFAAR is an even better substrate for the calpain 1 protease core than PLFAER, 100% cleavage preference
-
-
?
(EDANS)-EPLFAERK-(DABCYL) + H2O
(EDANS)-EPLFA + ERK-(DABCYL)
-
about 40% cleavage preference
-
-
?
(EDANS)-EPLFGERK-(DABCYL) + H2O
(EDANS)-EPLF + GERK-(DABCYL)
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less than 20% cleavage preference
-
-
?
(EDANS)-EPLFMERK-(DABCYL) + H2O
(EDANS)-EPLF + MERK-(DABCYL)
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the peptide sequence PLFMER is rapidly cleaved by the calpain 1 core at the F-M bond with about 45% cleavage preference
-
-
?
2-aminobenzoyl-EVYGMMY(3-NO2)-OH + H2O
2-aminobenzoyl-EVY + GMMY(3-NO2)-OH
-
-
-
-
?
4,4-difluoro-5,7-dimethyl-4-bora-31,4a-diaza-s-indacene-3-propioyl-labeled casein + H2O
?
-
-
-
-
?
5-([4,6-dichlorotriazin-2-yl]amino)fluorescin-labeled microtubule-associated protein 2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNIFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNIF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNIYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNIY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNLFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNLF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGNLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGNLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQIFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQIF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQLFGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQLF + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
7-methoxycoumarin-4-acetyl-GGGQLYGG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH + H2O
7-methoxycoumarin-4-acetyl-GGGQLY + GG-(Nbeta-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-KK-OH
-
-
-
-
?
acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O
acetyl-LLY + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
alphaII-spectrin + H2O
?
-
Fanconi anemia proteins play an important role in maintaining the stability of alphaII-spectrin in the cell by regulating its cleavage by mu-calpain
-
-
?
apoptosis inducing factor + H2O
truncated apoptosis inducing factor + ?
-
-
-
-
?
Bfl-1 protein + H2O
?
-
mu-calpain cleaves Bfl-1 at two major sites in its N-terminus releasing three fragments of 28000 Da, 12000 Da and 17500 Da
-
-
?
BH3-only Bcl2 interacting domain + H2O
?
-
BH3-only Bcl2 interacting domain is a direct target of a soluble active calpain 1 present in cells expressing hepatitis C virus proteins
-
-
?
Boc-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
Boc-Leu-Met + 7-amino-4-chloromethylcoumarin
-
10 microM, 20 min, 37 °C, with or without magnetic bead stimulation
-
-
?
caspase-7 + H2O
?
-
recombinant caspase-7 is directly cleaved and activated by calpain-1 within the large subunit of caspase-7 to produce the large subunit p18 and p17
-
-
?
dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala + H2O
dye-Gln-Gln-Gln-Glu-Val-Tyr + Gly-Met-Met-Pro-Arg-Asp-pSer-Ala
-
-
-
-
?
full-length glutamic acid decraboxylase67 + H2O
truncated glutamic acid decarboxylase67 + ?
Hsp70.1 + H2O
?
-
Hsp70.1 in the CA-1 tissue is an in-vivo substrate of activated mu-calpain, carbonylated Hsp70.1 in the CA-1 tissue by artificial oxidative stressors such as hydroxynonenal or hydrogen peroxide is much more vulnerable to the calpain cleavage
-
-
?
human epithelial growth factor receptor 2 + H2O
75000 Da fragment + 42000 Da fragment
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overexpression of calpain1 or activation of endogenous calpain during adhesion or trastuzumab treatment of trastuzumab-sensitive cells induces cleavage of cytoplasmic domains of human epithelial growth factor receptor 2/phospho-human epithelial growth factor receptor 2 protein
-
-
?
insulin-like growth factor binding protein-2 + H2O
?
-
the primary cleavage site in insulin-like growth factor binding protein-2 is localized to the non-conserved central linker regions
-
-
?
insulin-like growth factor binding protein-3 + H2O
?
-
the primary cleavage site in insulin-like growth factor binding protein-3 is localized to the non-conserved central linker regions. In vitro binding of mu-calpain to insulin-like growth factor binding protein-3 is a Ca2+-dependent reaction with a rapid on/off rate
-
-
?
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH + H2O
K-(5(6)-carboxyfluorescein)-EVY + GMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
-
-
-
-
?
L-plastin + H2O
?
-
L-plastin interaction with integrin is regulated through cleavage of beta-integrin by micro-calpain
-
-
?
mature apoptosis-inducing factor (62 kDa) + H2O
cleaved apoptosis-inducing factor (57 kDa) + ?
-
cleaved by the mitochondrial mu-calpain near its N-terminus
-
-
?
microtubule-associated protein 2 + H2O
?
-
calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2
-
-
?
mitochondrial major Ca2+ extruding pathway Na+/Ca2+ exchanger + H2O
?
-
cleaved by the mitochondrial mu-calpain
-
-
?
N-acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O
N-acetyl-LLY + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-succinyl-L-leucyl-L-valyl-L-tyrosinyl-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
neuronal calcium sensor-1 + H2O
?
-
mu-calpain cleavage of neuronal calcium sensor-1 occurs within an N-terminal pseudoEF-hand domain (at Lys36), which is unable to bind Ca2+
-
-
?
NR2 subunit of NMDA subtype of glutamate receptor + H2O
?
-
all three subtypes of NR2 subunits can be proteolyzed, cleavage of NR2A, NR2B and NR2C subunits is limited to their C-terminal region. Two cleavage sites at amino acids 1279 and 1330. Cleavage of NR2A-containing receptors does not alter basic NMDA receptor properties including calcium uptake, MK801 binding or electrophysiological measurement
-
-
?
p12 subunit of human DNA polymerase delta + H2O
?
-
the proteolysis of p12 by mu-calpain may be through a DNA polymerase delta4/PCNA complex. The p12/DNA polymerase delta is a target as a nuclear substrate of mu-calpain in calcium-triggered apoptosis
-
-
?
plasma membrane Ca2+-ATPase isoform 1 + H2O
?
-
readily and completely degraded by m-calpain
-
-
?
plasma membrane Ca2+-ATPase isoform 2 + H2O
?
-
slow hydrolysis only to large fragments
-
-
?
plasma membrane Ca2+-ATPase isoform 4 + H2O
?
-
slow hydrolysis only to large fragments
-
-
?
podoplanin + H2O
?
-
podoplanin stability is post-translationally regulated by calpain-1
-
-
?
prostacyclin synthase + H2O
?
calpain 1 cleaves and inactivates prostacyclin synthase in mesenteric arteries from diabetic mice. It cleaves the C-terminal domain of PGI2 synthase close to the catalytic site of the enzyme
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
-
calpain-cleavage of striatal-enriched protein tyrosine phosphatase 61 is NMDAR-dependent, Cdk5 enhances calpain-mediated cleavage of striatal-enriched protein tyrosine phosphatase 61, calpain cleaves recombinant striatal-enriched protein tyrosine phosphatase 46 in a dose-dependent manner
-
-
?
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Leu-L-Val + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Leu-L-Val-L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide + H2O
succinyl-L-Leu-L-Tyr + 4-methoxy-2-naphthylamine
-
-
-
-
?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-leucyl-L-methionine-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-leucyl-L-methionine + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Met + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
[2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 + H2O
[2-Abz]-Ser-Thr-Phe + Ala-Gln-Pro-[3-nitrotyrosine]-NH2
-
-
-
-
?
[4-((4-(dimethylamino)phenyl)azo)benzoic acid, succinimidyl ester]-Thr-Pro-Leu-Lys-Ser-Pro-Pro-Pro-Ser-Pro-Arg-[5-((2-aminoethyl)amino)naphthalene-1-sulfonic acid] + H2O
?
-
-
-
-
?
alpha-II-spectrin + H2O
?
-
-
calpain-specific spectrin cleaved products
-
?
alpha-spectrin + H2O
?
-
mu-calpain is neuroprotective in the early stage of excitotoxic injury. Activation and proteolysis of alpha-spectrin by mu-calpain preceds neuronal damage in the developing cerebral cortex induced by chronic treatament of methylmercury
-
-
?
apoptosis inducing factor + H2O
?
activated mitochondrial calpain 1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mitochondrial calpain 1 within the matrix cleaves complex I subunits and metabolic enzymes
-
-
?
apoptosis-inducing factor + H2O
?
-
although calpain I cleaves recombinant apoptosis-inducing factor in a cell free system, in intact cells under conditions where endogenous calpain is activated by either N-methyl-D-aspartate or N-methyl-N'-nitro-N-nitrosoguanidine administration, apoptosis-inducing factor is not cleaved
-
-
?
apoptosis-inducing factor + H2O
?
-
micro-calpain mediates the truncation and release of apoptosis-inducing factor from mitochondria following cisplatin treatment
-
-
?
apoptosis-inducing factor + H2O
?
-
calpain-mediated truncation of apoptosis-inducing factor is contingent upon poly(ADP-ribose) polymerase-1 activity
-
-
?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
-
-
-
-
?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
-
mitochondrial micro-calpain is the protease responsible for processing apoptosis-inducing factor prior to its release
-
-
?
ATP synthase-alpha (ATP5A1) + H2O
?
calpain-1 accumulation in mitochondria disrupts ATP synthase and induces ROS generation, which promotes diabetic cardiomyopathy
-
-
?
complex I subunits + H2O
?
activated mitochondrial calpain 1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mitochondrial calpain 1 within the matrix cleaves complex I subunits and metabolic enzymes
-
-
?
dynamin-like protein 1 + H2O
?
dynamin-like protein 1 (DLP1) is the key mitochondrial fission GTPase. It is a substrate of calpain which produced specific N-terminal DLP1 cleavage fragments. DLP1 is a physiological and Alzheimer's disease-relevant pathophysiological substrate of calpain in cells and in the brain. Calpain activation could contribute to reduced DLP1 levels and mitochondrial dynamics abnormalities and mitochondrial dysfunction in Alzheimer's disease
-
-
?
dynamin-like protein 1 + H2O
?
dynamin-like protein 1 (DLP1) is the key mitochondrial fission GTPase. It is a substrate of calpain which produced specific N-terminal DLP1 cleavage fragments
-
-
?
Frizzled-7 + H2O
?
-
calpain-1 is a regulator of Frizzled-7 turnover at the plasma membrane
-
-
?
full-length glutamic acid decraboxylase67 + H2O
truncated glutamic acid decarboxylase67 + ?
-
-
-
-
?
full-length glutamic acid decraboxylase67 + H2O
truncated glutamic acid decarboxylase67 + ?
-
in mu-calpain knockout mice, the level of truncated glutamic acid decarboxylase67 in the brain is greatly reduced compared with the wild-type. mu-Calpain is activated by neuronal stimulation and Ca2+-influx
-
-
?
gamma-filamin + H2O
?
-
phosphorylation of the filamin C-terminus domain by PKCalpha protects gamma-filamin against proteolysis by calpain 1 in COS cells
-
-
?
lysosomal associated membrane protein 2 + H2O
?
-
calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2
-
-
?
lysosomal associated membrane protein 2 + H2O
?
-
calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2
-
-
?
myelin-associated glycoprotein + H2O
?
-
calpain overexpression due to *OH stress, IFN-gamma stimulation, or Ca2+ influx is involved in C6 cell death
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
neuronal nitric oxide synthase + H2O
?
-
the mechanism of neuronal nitric oxide synthase activation is promoted by a calpain-mediated limited proteolysis through conversion of native 160 kDa nNOS into a fully active 130 kDa
-
-
?
recombinant procaspase-3 + H2O
?
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
recombinant procaspase-9 + H2O
?
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
RhoA + H2O
?
-
calpain cleaves RhoA and generates a form that inhibits integrin-induced stress fiber assembly and cell spreading
-
-
?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
-
primary role of calpain 1 and calpain 3 in meat tenderization
-
-
?
additional information
?
-
-
because the calcium concentration in postmortem muscle is high enough to activate mu-calpain, but not m-calpain, it seems reasonable to conclude that mu-calpain is responsible for postmortem degradation of calpastatin. Degradation of calpastatin by mu-calpain reduces calpain-inhibitory activity and is probably an important event in regulation of postmortem proteolysis, and, thus, meat tenderness
-
-
?
additional information
?
-
-
calpastatin could play an important role in preventing uncontrolled activity of l-calpain which otherwise may facilitate pulmonary hypertension, smooth muscle proliferation and apoptosis
-
-
?
additional information
?
-
-
translational expression of mu-calpain is up-regulated by 462.5% in MW white matter compared with controls. mu-Calpain activity and translational expression are not increased significantly in white matter from patients with Parkinsons or Alzheimer diseases compared with that of normal controls. Because calpain degrades all major myelin proteins, the increased activity and expression of this proteinase may play a critical role in myelinolysis in MS
-
-
?
additional information
?
-
-
calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons
-
-
?
additional information
?
-
-
calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis
-
-
?
additional information
?
-
pathological conditions associated with the gene of calpain 1: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, neurodegenerative disorders, cataracts, cancer
-
-
?
additional information
?
-
-
calpain 1 and 2 are required for RNA replication of echovirus 1
-
-
?
additional information
?
-
-
in the ischemic condition such as endometriosis, myoma of uterus and microscopic thrombosis, increasing of intracellular calcium ion concentration leads to the activation of l-calpain. Cleavage of integrin beta3 by over activated l-calpain may lead to an adverse effect on early pregnancy and to causing recurrent miscarriage
-
-
?
additional information
?
-
-
mu-calpain but not m-calpain can restore the cell migration rate. Knockdown of mu-calpain alters cell morphology with increased filopodial projections and a highly elongated tail that seems to prevent cell spreading and migration with reduced rear detachment ability. Knockdown of mu-calpain decreases the proteolytic products of filamin and talin, which are specifically rescued by overexpression of mucalpain but not m-calpain, suggesting that their proteolysis could be one of the key mechanisms by which mu-calpain regulates cell migration
-
-
?
additional information
?
-
-
mu-calpain prefers Leu, Val or Ile at the P2 position and Lys, Tyr, Arg, or Met at the P1 position
-
-
?
additional information
?
-
-
(EDANS)-EPAFAERK-(DABCYL), (EDANS)-EPLAAERK-(DABCYL), and (EDANS)-EPLFAEAK-(DABCYL) are very weak substrates for calpain 1 core
-
-
?
additional information
?
-
-
age-dependent myelin degeneration and proteolysis of oligodendrocyte proteins is associated with the activation of calpain-1
-
-
?
additional information
?
-
-
mu-Calpain regulates receptor activator of NF-kappaB ligand (RANKL)-supported osteoclastogenesis via NF-kappaB activation in RAW 264.7 cells
-
-
?
additional information
?
-
-
prednisolone suppresses ischemia-reperfusion injury of the rat liver. Its cytoprotective effect is partial, but is closely associated with inhibition of activation of mu-calpain and suppression of IL-beta and TNF-alpha transcription as well as with improved survival rate
-
-
?
additional information
?
-
-
the enzyme mediates tissue injury following post-ischemic and post-traumatic stress
-
-
?
additional information
?
-
-
mu-calpain, m-calpain, 20S proteasome, dipeptidyl peptidase II and III and soluble alanyl aminopeptidase are thought to induce lens opacification kinetically during cataract formation in Shumiya cataract rats through the intracellular turnover of lens proteins
-
-
?
additional information
?
-
-
role for mu-calpain isoform in the hypermeability of the diabetic endothelium
-
-
?
additional information
?
-
-
mitochondrial mu-calpain associates with ERp57, whereas, cytosolic mu-calpain does not associate with ERp57
-
-
?
additional information
?
-
enzyme is involved in myofibrillar protein degradation
-
-
?
additional information
?
-
-
enzyme is involved in myofibrillar protein degradation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alphaII-spectrin + H2O
?
-
Fanconi anemia proteins play an important role in maintaining the stability of alphaII-spectrin in the cell by regulating its cleavage by mu-calpain
-
-
?
apoptosis inducing factor + H2O
?
activated mitochondrial calpain 1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mitochondrial calpain 1 within the matrix cleaves complex I subunits and metabolic enzymes
-
-
?
apoptosis inducing factor + H2O
truncated apoptosis inducing factor + ?
-
-
-
-
?
apoptosis-inducing factor + H2O
?
-
although calpain I cleaves recombinant apoptosis-inducing factor in a cell free system, in intact cells under conditions where endogenous calpain is activated by either N-methyl-D-aspartate or N-methyl-N'-nitro-N-nitrosoguanidine administration, apoptosis-inducing factor is not cleaved
-
-
?
ATP synthase-alpha (ATP5A1) + H2O
?
calpain-1 accumulation in mitochondria disrupts ATP synthase and induces ROS generation, which promotes diabetic cardiomyopathy
-
-
?
caspase-7 + H2O
?
-
recombinant caspase-7 is directly cleaved and activated by calpain-1 within the large subunit of caspase-7 to produce the large subunit p18 and p17
-
-
?
complex I subunits + H2O
?
activated mitochondrial calpain 1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mitochondrial calpain 1 within the matrix cleaves complex I subunits and metabolic enzymes
-
-
?
dynamin-like protein 1 + H2O
?
dynamin-like protein 1 (DLP1) is the key mitochondrial fission GTPase. It is a substrate of calpain which produced specific N-terminal DLP1 cleavage fragments. DLP1 is a physiological and Alzheimer's disease-relevant pathophysiological substrate of calpain in cells and in the brain. Calpain activation could contribute to reduced DLP1 levels and mitochondrial dynamics abnormalities and mitochondrial dysfunction in Alzheimer's disease
-
-
?
Frizzled-7 + H2O
?
-
calpain-1 is a regulator of Frizzled-7 turnover at the plasma membrane
-
-
?
full-length glutamic acid decraboxylase67 + H2O
truncated glutamic acid decarboxylase67 + ?
-
in mu-calpain knockout mice, the level of truncated glutamic acid decarboxylase67 in the brain is greatly reduced compared with the wild-type. mu-Calpain is activated by neuronal stimulation and Ca2+-influx
-
-
?
mature apoptosis-inducing factor (62 kDa) + H2O
cleaved apoptosis-inducing factor (57 kDa) + ?
-
cleaved by the mitochondrial mu-calpain near its N-terminus
-
-
?
microtubule-associated protein 2 + H2O
?
-
calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2
-
-
?
mitochondrial major Ca2+ extruding pathway Na+/Ca2+ exchanger + H2O
?
-
cleaved by the mitochondrial mu-calpain
-
-
?
myelin-associated glycoprotein + H2O
?
-
calpain overexpression due to *OH stress, IFN-gamma stimulation, or Ca2+ influx is involved in C6 cell death
-
-
?
p12 subunit of human DNA polymerase delta + H2O
?
-
the proteolysis of p12 by mu-calpain may be through a DNA polymerase delta4/PCNA complex. The p12/DNA polymerase delta is a target as a nuclear substrate of mu-calpain in calcium-triggered apoptosis
-
-
?
prostacyclin synthase + H2O
?
calpain 1 cleaves and inactivates prostacyclin synthase in mesenteric arteries from diabetic mice. It cleaves the C-terminal domain of PGI2 synthase close to the catalytic site of the enzyme
-
-
?
RhoA + H2O
?
-
calpain cleaves RhoA and generates a form that inhibits integrin-induced stress fiber assembly and cell spreading
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
-
calpain-cleavage of striatal-enriched protein tyrosine phosphatase 61 is NMDAR-dependent, Cdk5 enhances calpain-mediated cleavage of striatal-enriched protein tyrosine phosphatase 61, calpain cleaves recombinant striatal-enriched protein tyrosine phosphatase 46 in a dose-dependent manner
-
-
?
alpha-spectrin + H2O
?
-
mu-calpain is neuroprotective in the early stage of excitotoxic injury. Activation and proteolysis of alpha-spectrin by mu-calpain preceds neuronal damage in the developing cerebral cortex induced by chronic treatament of methylmercury
-
-
?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
-
-
-
-
?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
-
mitochondrial micro-calpain is the protease responsible for processing apoptosis-inducing factor prior to its release
-
-
?
lysosomal associated membrane protein 2 + H2O
?
-
calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2
-
-
?
lysosomal associated membrane protein 2 + H2O
?
-
calpain 1 is responsible for lysosomal permeabilization by cleavage of the lysosomal associated membrane protein 2
-
-
?
neuronal nitric oxide synthase + H2O
?
-
the mechanism of neuronal nitric oxide synthase activation is promoted by a calpain-mediated limited proteolysis through conversion of native 160 kDa nNOS into a fully active 130 kDa
-
-
?
recombinant procaspase-3 + H2O
?
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
recombinant procaspase-9 + H2O
?
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
additional information
?
-
-
primary role of calpain 1 and calpain 3 in meat tenderization
-
-
?
additional information
?
-
-
because the calcium concentration in postmortem muscle is high enough to activate mu-calpain, but not m-calpain, it seems reasonable to conclude that mu-calpain is responsible for postmortem degradation of calpastatin. Degradation of calpastatin by mu-calpain reduces calpain-inhibitory activity and is probably an important event in regulation of postmortem proteolysis, and, thus, meat tenderness
-
-
?
additional information
?
-
-
calpastatin could play an important role in preventing uncontrolled activity of l-calpain which otherwise may facilitate pulmonary hypertension, smooth muscle proliferation and apoptosis
-
-
?
additional information
?
-
-
translational expression of mu-calpain is up-regulated by 462.5% in MW white matter compared with controls. mu-Calpain activity and translational expression are not increased significantly in white matter from patients with Parkinsons or Alzheimer diseases compared with that of normal controls. Because calpain degrades all major myelin proteins, the increased activity and expression of this proteinase may play a critical role in myelinolysis in MS
-
-
?
additional information
?
-
-
calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons
-
-
?
additional information
?
-
-
calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis
-
-
?
additional information
?
-
pathological conditions associated with the gene of calpain 1: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, neurodegenerative disorders, cataracts, cancer
-
-
?
additional information
?
-
-
calpain 1 and 2 are required for RNA replication of echovirus 1
-
-
?
additional information
?
-
-
in the ischemic condition such as endometriosis, myoma of uterus and microscopic thrombosis, increasing of intracellular calcium ion concentration leads to the activation of l-calpain. Cleavage of integrin beta3 by over activated l-calpain may lead to an adverse effect on early pregnancy and to causing recurrent miscarriage
-
-
?
additional information
?
-
-
mu-calpain but not m-calpain can restore the cell migration rate. Knockdown of mu-calpain alters cell morphology with increased filopodial projections and a highly elongated tail that seems to prevent cell spreading and migration with reduced rear detachment ability. Knockdown of mu-calpain decreases the proteolytic products of filamin and talin, which are specifically rescued by overexpression of mucalpain but not m-calpain, suggesting that their proteolysis could be one of the key mechanisms by which mu-calpain regulates cell migration
-
-
?
additional information
?
-
-
mu-calpain prefers Leu, Val or Ile at the P2 position and Lys, Tyr, Arg, or Met at the P1 position
-
-
?
additional information
?
-
-
age-dependent myelin degeneration and proteolysis of oligodendrocyte proteins is associated with the activation of calpain-1
-
-
?
additional information
?
-
-
mu-Calpain regulates receptor activator of NF-kappaB ligand (RANKL)-supported osteoclastogenesis via NF-kappaB activation in RAW 264.7 cells
-
-
?
additional information
?
-
-
prednisolone suppresses ischemia-reperfusion injury of the rat liver. Its cytoprotective effect is partial, but is closely associated with inhibition of activation of mu-calpain and suppression of IL-beta and TNF-alpha transcription as well as with improved survival rate
-
-
?
additional information
?
-
-
the enzyme mediates tissue injury following post-ischemic and post-traumatic stress
-
-
?
additional information
?
-
-
mu-calpain, m-calpain, 20S proteasome, dipeptidyl peptidase II and III and soluble alanyl aminopeptidase are thought to induce lens opacification kinetically during cataract formation in Shumiya cataract rats through the intracellular turnover of lens proteins
-
-
?
additional information
?
-
-
role for mu-calpain isoform in the hypermeability of the diabetic endothelium
-
-
?
additional information
?
-
enzyme is involved in myofibrillar protein degradation
-
-
?
additional information
?
-
-
enzyme is involved in myofibrillar protein degradation
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Mn2+
Sr2+
Ca2+
-
calcium-dependent, increase of amount of bound calpain 1 by calcium binding to titin
Ca2+
-
requires 0.053 mM Ca2+ for half-maximal activity. Activation by Ca2+ promotes the separation of the two subunits of the expressed recombinant protein
Ca2+
-
the primary event in Ca2+-activation corresponds to the binding of Ca2+ to eight interacting sites, of which are four in each of the two calpain subunits. Progressive binding of the metal iuon is linearly correlated with the dissociation of the proteinase, which reaches completion when all eight binding sites are occupied. The affinity for Ca2+ in the native heterodimeric calpain is increased 2fold in the isolated 80000 Da catalytic subunit, but it reaches a Kd-value consistent with the physiological concentration of Ca2+ only in the active autoproteolytically derived 75000 Da form. Binding of the Ca2+ in physiological conditions, and thus the formation of the 75000 Da subunit, can occur only in the presence of positive modulators, the natural activator protein or highly digestible substrates. As a result, both dissociation into the constituent subunits and the autoproteolytic conversion of the native 80000 Da subunit into the active 75000 Da subunit form can occur within the physiological fluctuations in Ca2+ concentrations
Ca2+
-
dependent on (0.002-0.02 mM). At resting [Ca2+], mu-calpain is present predominantly in its full-length, unautolysed/unactivated forms. Once activated, mu-calpain appears in its autolysed form. Endogenously expressed mu-calpain is activated within a physiological [Ca2+] range in a Ca2+- and time-dependent manner. Autolysed mu-calpain isoforms have a greater Ca2+ sensitivity than the full-length 80000 Da isoform
Ca2+
-
dependent on, dysfunctional mitochondria increase cytosolic calcium, thereby inducing calpain activation
Ca2+
-
mu-calpain is autolytically activated at micromolar Ca2+, mice muscle fibers that are partially excitation-contraction uncoupled by exposure to 0.005 mM Ca2+ for 3 min (no ATP) show the presence of autolytic activation of a proportion of the human mu-calpain present
Ca2+
-
the enzyme requires micromolar levels of Ca2+ for half-maximal activation
Ca2+
-
activation of mu-calpain requires micromolar calcium (0.4 mM used in assays)
Ca2+
-
half-maximal activation at 0.03 mM, maximal activation at 0.1 mM
Ca2+
-
Kd-value: 0.025 mM. 25% of the difference in Kd values between mu- and m-calpain can be ascribed to the N-terminal peptide of the large subunit, whereas the C-terminal EF-hand-containing domain IV accounts for 65% of the difference
Ca2+
-
mu-calpain is freely diffusible in the cytoplasm at resting Ca2+ concentrations but binds within seconds at high Ca2+ concentrations. Ca2+ concentration has to be raised to above 0.002 mM for more than 1 min to initiate detectable autolysis of mu-calpain and to activate appreciable proteolytic activity. If Ca2+ concentration is raised sufficiently for long enough to initiate substantial autolysis of mu-calpain, the Ca2+ sensitivity of the proteolytic activity is greatly increased and it remains active even at 300 nM Ca2+, with activity only ceasing if the Ca2+ concentration is decreased to about 50 nM Ca2+
Ca2+
-
dependent on (0.002-0.02 mM). At resting [Ca2+], mu-calpain is present predominantly in its full-length, unautolysed/unactivated forms. Once activated, mu-calpain appears in its autolysed form. Endogenously expressed mu-calpain is activated within a physiological [Ca2+] range in a Ca2+- and time-dependent manner. Autolysed mu-calpain isoforms have a greater Ca2+ sensitivity than the full-length 80000 Da isoform
Ca2+
-
incubation with 5 mM Ca2+ results in the activation of micro-calpain
Ca2+
-
micromolar (0.005-0.05 mM) Ca2+ concentrations are required for activation in vitro
Ca2+
-
dimeric calpain I requires 0.002 mM for half-maximal activation and 0.01 mM for maximal activation. The 70000 Da monomeric calpain I requires only 0.001 mM Ca2+ for half-maximal activity
Ca2+
-
calcium-dependent, increase of amount of bound calpain 1 by calcium binding to titin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
((1S)-1-((((1S)-1-benzyl-3-cyclopropylamino-2,3-di-oxopropyl)amino)carbonyl)-3-methylbutyl)carbamic acid 5-methoxy-3-oxapentyl ester
-
SNJ-1945
(2R)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-6-oxopiperidine-2-carboxamide
-
(2S)-2-[[(4-fluorophenyl)sulfonyl]amino]-N-[(3S)-2-hydroxytetrahydrofuran-3-yl]-3-methylbutanamide
-
-
(2S,3S)-trans-epoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester
-
broad-spectrum calpain inhibitor
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(10H-phenothiazin-2-yloxy)acetyl]-L-threonyl-L-leucinate
-
-
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(2S)-2-[[(10H-phenothiazin-2-yloxy)acetyl]amino]butanoyl]-L-leucinate
-
-
(3S)-3-[[N-(10H-phenothiazin-2-ylcarbonyl)-L-norvalyl]amino]tetrahydrofuran-2-yl acetate
-
BN-82270
(4R)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-benzyl-1-methyl-2-oxoimidazolidine-4-carboxamide
-
(4S)-3-[(4-methylphenyl)sulfonyl]-N-(1-oxo-3-phenylpropan-2-yl)-1,3-thiazolidine-4-carboxamide
-
-
(4S)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-4-methyl-5-oxo-D-prolinamide
-
(6S,9S,16R)-6-(hydroxymethyl)-9-(2-methylpropyl)-16-phenyl-2,15-dioxa-7,10,13-triazabicyclo[16.2.2]docosa-1(20),18,21-triene-8,11,14-trione
-
-
(6S,9S,16R)-9-(2-methylpropyl)-8,11,14-trioxo-16-phenyl-2,15-dioxa-7,10,13-triazabicyclo[16.2.2]docosa-1(20),18,21-triene-6-carbaldehyde
-
less potent inhibitor with greater than 2fold selectivity for ovine calpain 1 over calpain 2
(7S,10S,13S,26S)-13,26-dibenzyl-7-methyl-10-(propan-2-yl)-5,7,8,10,11,13,14,25,26,28-decahydrotetrabenzo[k,m,t,v][1,4,7,10,15,18]hexaazacyclotetracosine-6,9,12,15,24,27-hexone
-
-
(7S,10S,17R)-10-(2-methylpropyl)-9,12,15-trioxo-17-phenyl-2,16-dioxa-8,11,14-triazabicyclo[17.2.2]tricosa-1(21),19,22-triene-7-carbaldehyde
-
potent inhibitor of calpain with greater than 7fold selectivity for ovine calpain 2 over ovine calpain 1
(7S,10S,17R)-7-(hydroxymethyl)-10-(2-methylpropyl)-17-phenyl-2,16-dioxa-8,11,14-triazabicyclo[17.2.2]tricosa-1(21),19,22-triene-9,12,15-trione
-
-
(8S,11S,18R)-11-(2-methylpropyl)-10,13,16-trioxo-18-phenyl-2,17-dioxa-9,12,15-triazabicyclo[18.2.2]tetracosa-1(22),20,23-triene-8-carbaldehyde
-
-
(8S,11S,18R)-8-(hydroxymethyl)-11-(2-methylpropyl)-18-phenyl-2,17-dioxa-9,12,15-triazabicyclo[18.2.2]tetracosa-1(22),20,23-triene-10,13,16-trione
-
-
(9R,12S,19R)-12-(2-methylpropyl)-11,14,17-trioxo-19-phenyl-2,18-dioxa-7-thia-10,13,16-triazabicyclo[19.2.2]pentacosa-1(23),21,24-triene-9-carbaldehyde
-
-
(9R,12S,19R)-9-(hydroxymethyl)-12-(2-methylpropyl)-19-phenyl-2,18-dioxa-7-thia-10,13,16-triazabicyclo[19.2.2]pentacosa-1(23),21,24-triene-11,14,17-trione
-
-
([(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]oxy)ethynyl (2Z)-[(3R)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
-
-
1,2-bis(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetra(acetoxymethyl) ester
-
-
1-(2-chloro-4-hydroxyphenyl)-4-oxo-7-(pyridin-4-yl)-1,4-dihydroquinoline-3-carboxamide
-
-
1-(2-chlorobenzyl)-N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[3,4-dioxo-1-phenyl-4-(phenylamino)butan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[4-(cyclobutylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[4-(methoxyamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
1-benzyl-N-[4-[(4-fluorophenyl)amino]-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
2-methyl-N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
-
3,4-dichlorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 56 nM
3,4-dichlorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 56 nM
3-([4-[2-(methoxymethoxy)phenyl]-4-oxobutanoyl]amino)-2-oxo-4-phenylbutanamide
-
reversible inhibitor
3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoic acid
-
reversible inhibitor
3-acetyl-2-[(2,4-dichlorophenyl)amino]-8-(trifluoromethyl)quinolin-4(1H)-one
-
-
3-acetyl-2-[[3,5-bis(trifluoromethyl)phenyl]amino]-5,8-difluoroquinolin-4(1H)-one
-
-
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
-
-
3-acetyl-6-chloro-8-(trifluoromethyl)-2-[[4-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
-
-
3-acetyl-7,8-dichloro-2-[[3-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(2-fluoro-5-methylphenyl)amino]-5-(trifluoromethyl)quinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(4-chloro-2-fluorophenyl)amino]-5-methylquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-5-methyl-2-[(2,3,4-trifluorophenyl)amino]quinolin-4(1H)-one
-
-
3-acetyl-8-chloro-5-methyl-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
-
-
4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoic acid
-
reversible inhibitor
4-fluorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 29 nM
4-fluorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 50 nM
4-nitrophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 47 nM
4-nitrophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 50 nM
4-[([(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]oxy)methyl]benzyl (2Z)-[(3R)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
-
-
5-azanylidyne-N-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]-L-norvalyl-L-arginyl-L-tryptophanamide
-
irreversible inhibitor
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]-1H-pyrrole-2-carboxamide
-
CAT0059
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]furan-2-carboxamide
-
-
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]thiophene-2-carboxamide
-
-
Al3+
-
inactivates enzyme from smooth muscle at millimolar concentrations of Ca2+, calpain 1 and 2
benzyl (2Z)-[(3S)-3-sec-butyl-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetate
-
-
benzyl [(6S,9S,12S)-6-formyl-9-(2-methylpropyl)-8,11-dioxo-2-oxa-7,10-diazabicyclo[12.2.2]octadeca-1(16),14,17-trien-12-yl]carbamate
-
-
benzyl [(7S,10S,13S)-7-formyl-10-(2-methylpropyl)-9,12-dioxo-2-oxa-8,11-diazabicyclo[13.2.2]nonadeca-1(17),15,18-trien-13-yl]carbamate
-
CAT811
benzyl [(8S,11S,14S)-8-formyl-11-(2-methylpropyl)-10,13-dioxo-2-oxa-9,12-diazabicyclo[14.2.2]icosa-1(18),16,19-trien-14-yl]carbamate
-
-
butyl (2Z)-[(3S)-3-(butan-2-yl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
-
-
calpastatin 1
-
calpain 1 is under constant inhibiting effect of active calpastatin 1
-
CP1B peptide
-
a 20-mer peptide truncated from region B of calpastatin inhibitory domain 1, 1000fold more selective for mu-calpain than cathepsin L
-
cystatin
-
engineered cystatins. Recombinant hybrids of human stefin B with KS2 and DELTAL110 deletion mutants of chicken cystatin-KD2 hybrids. Substitution of the N-terminal contact region of stefin B by ther corresponding KD2 sequence results in a calpain inhibitor with a Ki-value of 188 nM. Deletion of L110 improves inhibition 4 to 8fold. All engineered cystatins are temporary inhibitors
-
dimethyl (2S,2'S)-2,2'-[biphenyl-2,2'-diylbis(carbonylimino)]bis(3-phenylpropanoate)
-
-
DPMSSTYIEELGKREVTIPPKYRELLA
-
2 hot spots are detected in which the residues critical for inhibitory function are clustered: Leu11-Gly12 and Thr17-Ile18-Pro19
ethyl 3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoate
-
reversible inhibitor
ethyl 4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoate
-
reversible inhibitor
heat shock protein 90
-
incubation of calpain-1 at a molar ratio of 1:1 with heat shock protein 90, at increasing Ca2+ concentrations, results in a significant decrease of calpain proteolytic activity at [Ca2+] up to 0.04 mM. At higher Ca2+ concentrations, the inhibiting effect of heat shock protein 90 is no more detectable
-
methyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 89 nM
methyl (2Z)-[(3S)-3-sec-butyl-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetate
-
-
methyl (3S)-4-cyclohexyl-3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxobutanoate
-
IC50: 1000 nM
methyl (S,S,Z)-(3-sec-butyl-1-oxo-2,3-dihydro-1H-isoquinolin-4-ylidene)acetate
-
strong inhibitor
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-isoleucyl-L-isoleucinate
-
-
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-isoleucyl-L-isoleucyl-L-isoleucinate
-
-
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-leucyl-L-phenylalaninate
-
-
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-valyl-L-phenylalaninate
-
-
methyl N-[[2'-([(2S)-1-[(2'-aminobiphenyl-2-yl)amino]-1-oxo-3-phenylpropan-2-yl]carbamoyl)biphenyl-2-yl]carbonyl]-L-phenylalanyl-L-valinate
-
-
N'-((1S,2R)-1-benzyl-3-[(3,5-dimethoxybenzyl)amino]-2-hydroxypropyl)-N,N-dipropylbenzene-1,3-dicarboxamide
-
IC50: 20 nM
N-((1S)-1-benzyl-2,3-dioxo-3-[(2-phenylethyl)amino]propyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 63 nM
N-((1S)-1-benzyl-3-[(1-methylethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 205 nM
N-((1S)-1-benzyl-3-[(2-methoxyethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 200 nM
N-((1S)-1-benzyl-3-[(cyclopropylmethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 286 nM
N-((1S)-1-[(butylamino)(oxo)acetyl]-3-methylbutyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(1-benzothiophen-2-ylcarbonyl)piperidine-4-carboxamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(2,2-dimethylpropyl)-5-oxo-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(cyclohexylmethyl)-5-oxo-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-6-oxo-1,6-dihydropyridine-2-carboxamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-[(4-methylphenyl)sulfonyl]-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-[2-methoxy-6-(trifluoromethyl)benzyl]-5-oxo-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-2-benzyl-1,2-thiazolidine-3-carboxamide 1,1-dioxide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-2-[(E)-2-[4-[(diethylamino)methyl]phenyl]ethenyl]benzamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-1,4-dihydroquinoline-2-carboxamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-4H-chromene-2-carboxamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-4-methyl-6-methylidene-1,6-dihydropyridine-3-carboxamide
-
reversible inhibitor
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-(pyridin-4-ylmethyl)-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[2-(trifluoromethoxy)benzyl]-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[2-(trifluoromethyl)benzyl]-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[3-(trifluoromethoxy)benzyl]-D-prolinamide
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[3-(trifluoromethyl)benzyl]-D-prolinamide
-
N-acetyl-Leu-Leu-norleucinal
-
2-fold increase in Tat levels after pre-treating with ALLN, 10 microM
N-benzyloxycarbonyl-L-leucyl-L-leucyl-L-tyrosyl fluoromethylketone
-
broad-spectrum calpain inhibitor
N-[(1S)-1-benzyl-2,3-dioxo-3-(pentylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 150 nM
N-[(1S)-1-benzyl-2,3-dioxo-3-(prop-2-en-1-ylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 200 nM
N-[(1S)-1-benzyl-3-(benzylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 81 nM
N-[(1S)-1-benzyl-3-(butylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
-
N-[(1S)-1-benzyl-3-(ethylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
IC50: 340 nM
N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2,4]benzothiadiazine-3-carboxamide 1,1-dioxide
-
-
N-[(2S)-1-[[(3S)-2-hydroxytetrahydrofuran-3-yl]amino]-1-oxopentan-2-yl]-10H-phenothiazine-2-carboxamide
-
BN-82204
N-[(2S)-3,4-dioxo-1-phenyl-4-([3-[(phenylsulfonyl)amino]propyl]amino)butan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
reversible inhibitor
N-[(2S)-4-(2-benzylhydrazinyl)-3,4-dioxo-1-phenylbutan-2-yl]-N2-[(benzyloxy)carbonyl]-L-leucinamide
-
reversible inhibitor
N-[(2S)-4-(butylamino)-3,4-dioxo-1-phenylbutan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
-
reversible inhibitor
N-[(benzyloxy)carbonyl]-L-leucyl-N-[(2S)-4-fluoro-1-(4-hydroxyphenyl)-3-oxobutan-2-yl]-L-leucinamide
-
irreversible inhibitor
N-[1-(4-bromophenyl)-4-(ethylamino)-3,4-dioxobutan-2-yl]-N2-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucinamide
-
reversible inhibitor
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-1-(1-methyl-1H-pyrazol-4-yl)-5-oxo-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-1-(2,3-dihydro-1H-inden-2-yl)-5-oxo-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethoxy)-6-(trifluoromethyl)benzyl]-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethoxy)benzyl]-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethyl)benzyl]-D-prolinamide
-
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
-
N-[[(1R)-1-phenyl-2-(4-propoxyphenyl)ethoxy]carbonyl]glycyl-N-[(2S)-1-hydroxypentan-2-yl]-L-leucinamide
-
-
N-[[(1R)-1-phenyl-2-(4-propoxyphenyl)ethoxy]carbonyl]glycyl-N-[(2S)-1-oxopentan-2-yl]-L-leucinamide
-
potent inhibitor with more than 2.5fold selectivity for ovine calpain 1 over ovine calpain 2
N-[[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]-L-histidyl-L-arginyl-L-tryptophanamide
-
irreversible inhibitor
N2-[(2S)-2-([[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]amino)pent-4-enoyl]-L-arginyl-L-tryptophanamide
-
irreversible inhibitor
N2-[(benzyloxy)carbonyl]-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-L-leucinamide
-
reversible inhibitor
phenyl (2-[(3-([(1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 76 nM
phenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
-
IC50: 40 nM
phenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
-
IC50: 35 nM
ritonavir
-
also inhibits calcium-stimulated calpain activity in PC12 cells in situ. Ritonavir or analogues of the drug should by investigated as cytoprotective agents in conditions where cell death or injury is mediated via calpain activation
calpastatin
-
the occurrence of a complex between heat shock protein 90 and calpain-1, in which the protease is still activable, can prevent the complete inhibition of the protease even in the presence of high calpastatin levels
-
calpastatin
-
mitochondrial mu-calpain is tightly regulated by its endogenous inhibitor calpastatin
-
calpastatin
-
inhibition of mu-calpain is higher at 295 mM NaCl than at 165 mM. Inhibition is not altered by pH from pH 6.0-7.5
-
calpastatin
-
oxidation lowers calpastatin inhibition of mu-calpain at al pH and ionic strength combinations
-
additional information
-
FANCA and FANCG proteins bind directly to mu-calpain, this binding may lead to inhibition of mu-calpain activity in normal cells
-
additional information
-
specific capn1 shRNA reduces expression of the targeted isoform
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
angiotensin II
-
1.2-fold increased activity of calpain-1, influence in expression of calpain-1
Ca2+
-
required for activation of mu-calpain. Membrane-binding of mu-calpain is Ca2+-dependent. Membrane binding of mu-calpain is due to the exposed hydrophobic surface of the active site conformation and does not reduce the Ca2+ requirement for activation
endotoxin
-
treatment with 12 mg/kg endotoxin increases diaphragm calpain activity and active calpain I protein
-
NS5A protein
-
the nonstructural hepatitis C virus protein NS5Ais sufficient to activate a calpain 1
-
additional information
-
HRSP12 (UK114) stimulates the hydrolysis activity of Calpain1
-
additional information
-
no influence on expression of calpain-1 by mechanical stimulation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
2-aminobenzoyl-EVYGMMY(3-NO2)-OH
-
pH and temperature not specified in the publication
0.00074
4,4-difluoro-5,7-dimethyl-4-bora-31,4a-diaza-s-indacene-3-propioyl-labeled casein
-
pH and temperature not specified in the publication
-
0.0131
fluorescin thiocarbamoyl-labeled casein
-
pH and temperature not specified in the publication
-
0.0046
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
-
pH and temperature not specified in the publication
0.37
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
0.19
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.46
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin
-
pH and temperature not specified in the publication
0.2
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.2
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
1.2
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.43
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
4.7
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
5.9
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.002
succinyl-bovine serum albumin
-
pH and temperature not specified in the publication
-
0.284
succinyl-insulin B
-
pH and temperature not specified in the publication
-
0.063
succinyl-protamine
-
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.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
2-aminobenzoyl-EVYGMMY(3-NO2)-OH
-
pH and temperature not specified in the publication
0.11
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
-
pH and temperature not specified in the publication
0.52
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
0.02
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.07
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin
-
pH and temperature not specified in the publication
0.29
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.029
succinyl-L-Leu-L-Leu-L-Val-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.062
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.12
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide
-
pH and temperature not specified in the publication
0.37
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
0.49
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
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
0.000064
(2R)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-6-oxopiperidine-2-carboxamide
pH and temperature not specified in the publication
0.000101
(4R)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-benzyl-1-methyl-2-oxoimidazolidine-4-carboxamide
pH and temperature not specified in the publication
0.00005
(4S)-N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-4-methyl-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000073
1-(2-chlorobenzyl)-N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00007
1-benzyl-N-[3,4-dioxo-1-phenyl-4-(phenylamino)butan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00011
1-benzyl-N-[4-(cyclobutylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00013
1-benzyl-N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000165
1-benzyl-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00436
1-benzyl-N-[4-(methoxyamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000048
1-benzyl-N-[4-[(4-fluorophenyl)amino]-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000081
1-[(4-methylphenyl)sulfonyl]-N-(1-oxo-3-phenylpropan-2-yl)-D-prolinamide
-
pH and temperature not specified in the publication
0.0000085
3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoic acid
-
pH and temperature not specified in the publication
0.00005
4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoic acid
-
pH and temperature not specified in the publication
0.017
acetyl-DPMSSTYIEE-betaAla-GKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.0024
acetyl-DPMSSTYIEELGKREVT-betaAla-PPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.0000002
acetyl-DPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.00000019
acetyl-RRMKWKKDPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
0.000026
acetyl-SSTTYIEELGKREVTIPPKYR-NH2
-
pH and temperature not specified in the publication
0.0018
ethyl 3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoate
-
pH and temperature not specified in the publication
0.01
ethyl 4-(4-bromophenyl)-3-([N-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucyl]amino)-2-oxobutanoate
-
IC50 above 0.01 mM, pH and temperature not specified in the publication
0.000046
N-(1-amino-1,2-dioxoheptan-3-yl)-1-benzyl-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000009
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(1-benzothiophen-2-ylcarbonyl)piperidine-4-carboxamide
-
pH and temperature not specified in the publication
0.00135
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(2,2-dimethylpropyl)-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000268
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-(cyclohexylmethyl)-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000039
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000528
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-5-oxo-L-prolinamide
pH and temperature not specified in the publication
0.000082
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-benzyl-6-oxo-1,6-dihydropyridine-2-carboxamide
pH and temperature not specified in the publication
0.000129
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-[(4-methylphenyl)sulfonyl]-D-prolinamide
pH and temperature not specified in the publication
0.000036
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-1-[2-methoxy-6-(trifluoromethyl)benzyl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000268
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-2-benzyl-1,2-thiazolidine-3-carboxamide 1,1-dioxide
pH and temperature not specified in the publication
0.000027
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-2-[(E)-2-[4-[(diethylamino)methyl]phenyl]ethenyl]benzamide
-
pH and temperature not specified in the publication
0.00018
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-(pyridin-4-ylmethyl)-D-prolinamide
pH and temperature not specified in the publication
0.000057
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[2-(trifluoromethoxy)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.000059
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[2-(trifluoromethyl)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.000125
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[3-(trifluoromethoxy)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.000026
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-5-oxo-1-[3-(trifluoromethyl)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.0000047
N-[(2S)-4-(2-benzylhydrazinyl)-3,4-dioxo-1-phenylbutan-2-yl]-N2-[(benzyloxy)carbonyl]-L-leucinamide
-
pH and temperature not specified in the publication
0.00002
N-[1-(4-bromophenyl)-4-(ethylamino)-3,4-dioxobutan-2-yl]-N2-[5-(1,2-dithiolan-3-yl)pentanoyl]-L-leucinamide
-
pH and temperature not specified in the publication
0.00053
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-1-(1-methyl-1H-pyrazol-4-yl)-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.000545
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-1-(2,3-dihydro-1H-inden-2-yl)-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.00024
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethoxy)-6-(trifluoromethyl)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.00005
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethoxy)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.00009
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-1-[2-(trifluoromethyl)benzyl]-D-prolinamide
pH and temperature not specified in the publication
0.00097
N-[4-(cyclopropylamino)-3,4-dioxo-1-phenylbutan-2-yl]-5-oxo-D-prolinamide
pH and temperature not specified in the publication
0.0002
N2-[(benzyloxy)carbonyl]-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-L-leucinamide
-
pH and temperature not specified in the publication
0.000093
acetyl-TYIEELGKREVTIPPKYR-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.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00088
(2S)-2-[[(4-fluorophenyl)sulfonyl]amino]-N-[(3S)-2-hydroxytetrahydrofuran-3-yl]-3-methylbutanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0007
(2S,5S)-5-benzyl-6-hydroxy-2-(2-methylpropyl)morpholin-3-one
Homo sapiens
-
pH and temperature not specified in the publication
0.000038
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(10H-phenothiazin-2-yloxy)acetyl]-L-threonyl-L-leucinate
Homo sapiens
-
pH and temperature not specified in the publication
0.000089
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(2S)-2-[[(10H-phenothiazin-2-yloxy)acetyl]amino]butanoyl]-L-leucinate
Homo sapiens
-
pH and temperature not specified in the publication
0.001
(3S)-3-[[N-(10H-phenothiazin-2-ylcarbonyl)-L-norvalyl]amino]tetrahydrofuran-2-yl acetate
Homo sapiens
-
IC50 above 0.001 mM, pH and temperature not specified in the publication
0.013
(6S,9S,16R)-6-(hydroxymethyl)-9-(2-methylpropyl)-16-phenyl-2,15-dioxa-7,10,13-triazabicyclo[16.2.2]docosa-1(20),18,21-triene-8,11,14-trione
Ovis aries
-
pH and temperature not specified in the publication
0.0004
(6S,9S,16R)-9-(2-methylpropyl)-8,11,14-trioxo-16-phenyl-2,15-dioxa-7,10,13-triazabicyclo[16.2.2]docosa-1(20),18,21-triene-6-carbaldehyde
Ovis aries
-
pH and temperature not specified in the publication
0.029
(7S,10S,13S,26S)-13,26-dibenzyl-7-methyl-10-(propan-2-yl)-5,7,8,10,11,13,14,25,26,28-decahydrotetrabenzo[k,m,t,v][1,4,7,10,15,18]hexaazacyclotetracosine-6,9,12,15,24,27-hexone
Homo sapiens
-
pH and temperature not specified in the publication
0.00022
(7S,10S,17R)-10-(2-methylpropyl)-9,12,15-trioxo-17-phenyl-2,16-dioxa-8,11,14-triazabicyclo[17.2.2]tricosa-1(21),19,22-triene-7-carbaldehyde
Ovis aries
-
pH and temperature not specified in the publication
0.00175
(7S,10S,17R)-7-(hydroxymethyl)-10-(2-methylpropyl)-17-phenyl-2,16-dioxa-8,11,14-triazabicyclo[17.2.2]tricosa-1(21),19,22-triene-9,12,15-trione
Ovis aries
-
pH and temperature not specified in the publication
0.00017
(8S,11S,18R)-11-(2-methylpropyl)-10,13,16-trioxo-18-phenyl-2,17-dioxa-9,12,15-triazabicyclo[18.2.2]tetracosa-1(22),20,23-triene-8-carbaldehyde
Ovis aries
-
pH and temperature not specified in the publication
0.00134
(8S,11S,18R)-8-(hydroxymethyl)-11-(2-methylpropyl)-18-phenyl-2,17-dioxa-9,12,15-triazabicyclo[18.2.2]tetracosa-1(22),20,23-triene-10,13,16-trione
Ovis aries
-
pH and temperature not specified in the publication
0.00315
(9R,12S,19R)-12-(2-methylpropyl)-11,14,17-trioxo-19-phenyl-2,18-dioxa-7-thia-10,13,16-triazabicyclo[19.2.2]pentacosa-1(23),21,24-triene-9-carbaldehyde
Ovis aries
-
pH and temperature not specified in the publication
0.05
(9R,12S,19R)-9-(hydroxymethyl)-12-(2-methylpropyl)-19-phenyl-2,18-dioxa-7-thia-10,13,16-triazabicyclo[19.2.2]pentacosa-1(23),21,24-triene-11,14,17-trione
Ovis aries
-
pH and temperature not specified in the publication
59
([(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]oxy)ethynyl (2Z)-[(3R)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
Sus scrofa
-
-
0.0005
1-(2-chloro-4-hydroxyphenyl)-4-oxo-7-(pyridin-4-yl)-1,4-dihydroquinoline-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000006
2-methyl-N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.000056
3,4-dichlorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 56 nM
0.000056
3,4-dichlorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 56 nM
0.00034
3-([4-[2-(methoxymethoxy)phenyl]-4-oxobutanoyl]amino)-2-oxo-4-phenylbutanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0192
3-acetyl-2-[(2,4-dichlorophenyl)amino]-8-(trifluoromethyl)quinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-2-[(3-fluorophenyl)amino]-8-phenylquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-2-[(4-chlorophenyl)amino]-5,8-difluoroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-2-[(4-tert-butylphenyl)amino]-5,8-difluoroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00369 - 0.00743
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
0.03
3-acetyl-2-[[3,5-bis(trifluoromethyl)phenyl]amino]-5,8-difluoroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-6,8-difluoro-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00316 - 0.00464
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-4(1H)-one
0.00239 - 0.00373
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
0.03
3-acetyl-6-chloro-8-(trifluoromethyl)-2-[[4-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-7,8-dichloro-2-[[3-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.000277 - 0.00306
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
0.03
3-acetyl-8-chloro-2-[(2-fluoro-5-methylphenyl)amino]-5-(trifluoromethyl)quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-8-chloro-2-[(3-methylphenyl)amino]-5-nitroquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-8-chloro-2-[(4-chloro-2-fluorophenyl)amino]-5-methylquinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-8-chloro-5-fluoro-2-(phenylamino)quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-8-chloro-5-methyl-2-[(2,3,4-trifluorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.03
3-acetyl-8-chloro-5-methyl-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
IC50 above 0.03 mM, using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.000029
4-fluorophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 29 nM
0.00005
4-fluorophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 50 nM
0.000047
4-nitrophenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 47 nM
0.00005
4-nitrophenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 50 nM
5
4-[([(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]oxy)methyl]benzyl (2Z)-[(3R)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]ethanoate
Homo sapiens
-
-
0.00033
5-azanylidyne-N-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]-L-norvalyl-L-arginyl-L-tryptophanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00029
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]-1H-pyrrole-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00096
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]furan-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00044
5-formyl-N-[(2S)-3-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxobutan-2-yl]thiophene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00019
acetyl-Leu-Leu-Nle-CHO
Rattus norvegicus
-
pH and temperature not specified in the publication
85
benzyl (2Z)-[(3S)-3-sec-butyl-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetate
Sus scrofa
-
-
0.0004
benzyl [(6S,9S,12S)-6-formyl-9-(2-methylpropyl)-8,11-dioxo-2-oxa-7,10-diazabicyclo[12.2.2]octadeca-1(16),14,17-trien-12-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.00022
benzyl [(7S,10S,13S)-7-formyl-10-(2-methylpropyl)-9,12-dioxo-2-oxa-8,11-diazabicyclo[13.2.2]nonadeca-1(17),15,18-trien-13-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.00017
benzyl [(8S,11S,14S)-8-formyl-11-(2-methylpropyl)-10,13-dioxo-2-oxa-9,12-diazabicyclo[14.2.2]icosa-1(18),16,19-trien-14-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.000008
calpain inhibitor III
Rattus norvegicus
-
pH and temperature not specified in the publication
0.0000075
calpain inhibitor VI
Rattus norvegicus
-
pH and temperature not specified in the publication
0.000064
dimethyl (2S,2'S)-2,2'-[biphenyl-2,2'-diylbis(carbonylimino)]bis(3-phenylpropanoate)
Homo sapiens
-
pH and temperature not specified in the publication
0.000089
methyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 89 nM
0.000025
methyl (2Z)-[(3S)-3-sec-butyl-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetate
Sus scrofa
-
-
0.001
methyl (3S)-4-cyclohexyl-3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxobutanoate
Homo sapiens
-
IC50: 1000 nM
0.000025
methyl (S,S,Z)-(3-sec-butyl-1-oxo-2,3-dihydro-1H-isoquinolin-4-ylidene)acetate
Homo sapiens
-
pH and temperature not specified in the publication
0.000447
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-isoleucyl-L-isoleucinate
Sus scrofa
-
-
0.000159
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-isoleucyl-L-isoleucyl-L-isoleucinate
Sus scrofa
-
-
0.000066
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-leucyl-L-phenylalaninate
Sus scrofa
-
-
0.000626
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-valyl-L-phenylalaninate
Sus scrofa
-
-
0.000000087
methyl N-[[2'-([(2S)-1-[(2'-aminobiphenyl-2-yl)amino]-1-oxo-3-phenylpropan-2-yl]carbamoyl)biphenyl-2-yl]carbonyl]-L-phenylalanyl-L-valinate
Homo sapiens
-
pH and temperature not specified in the publication
0.00002
N'-((1S,2R)-1-benzyl-3-[(3,5-dimethoxybenzyl)amino]-2-hydroxypropyl)-N,N-dipropylbenzene-1,3-dicarboxamide
Homo sapiens
-
IC50: 20 nM
0.000063
N-((1S)-1-benzyl-2,3-dioxo-3-[(2-phenylethyl)amino]propyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 63 nM
0.000205
N-((1S)-1-benzyl-3-[(1-methylethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 205 nM
0.0002
N-((1S)-1-benzyl-3-[(2-methoxyethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 200 nM
0.000286
N-((1S)-1-benzyl-3-[(cyclopropylmethyl)amino]-2,3-dioxopropyl)-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 286 nM
0.00071
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-1,4-dihydroquinoline-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-4H-chromene-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0028
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-4-methyl-6-methylidene-1,6-dihydropyridine-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00015
N-[(1S)-1-benzyl-2,3-dioxo-3-(pentylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 150 nM
0.0002
N-[(1S)-1-benzyl-2,3-dioxo-3-(prop-2-en-1-ylamino)propyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 200 nM
0.000081
N-[(1S)-1-benzyl-3-(benzylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 81 nM
0.00034
N-[(1S)-1-benzyl-3-(ethylamino)-2,3-dioxopropyl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
IC50: 340 nM
0.000028
N-[(2S)-1-oxo-3-phenylpropan-2-yl]-7,8-dihydro-2H-[1,4]dioxino[2,3-g][1,2,4]benzothiadiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.000023
N-[(2S)-1-[[(3S)-2-hydroxytetrahydrofuran-3-yl]amino]-1-oxopentan-2-yl]-10H-phenothiazine-2-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000035
N-[(2S)-3,4-dioxo-1-phenyl-4-([3-[(phenylsulfonyl)amino]propyl]amino)butan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.00005
N-[(2S)-4-(butylamino)-3,4-dioxo-1-phenylbutan-2-yl]-2-ethyl-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazine-3-carboxamide 1,1-dioxide
Homo sapiens
-
pH and temperature not specified in the publication
0.0032
N-[[(1R)-1-phenyl-2-(4-propoxyphenyl)ethoxy]carbonyl]glycyl-N-[(2S)-1-hydroxypentan-2-yl]-L-leucinamide
Ovis aries
-
pH and temperature not specified in the publication
0.00005
N-[[(1R)-1-phenyl-2-(4-propoxyphenyl)ethoxy]carbonyl]glycyl-N-[(2S)-1-oxopentan-2-yl]-L-leucinamide
Ovis aries
-
pH and temperature not specified in the publication
0.00078
N2-[(2S)-2-([[(2R,3R)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]amino)pent-4-enoyl]-L-arginyl-L-tryptophanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.000076
phenyl (2-[(3-([(1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 76 nM
0.00004
phenyl (2-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]ethyl)amidosulfite
Homo sapiens
-
IC50: 40 nM
0.000035
phenyl (3-[(3-([(2-ethyl-1,1-dioxido-3,4,7,8-tetrahydro-2H-[1,4]dioxino[2,3-g][1,2]benzothiazin-3-yl)carbonyl]amino)-2-oxo-4-phenylbutanoyl)amino]propyl)amidosulfite
Homo sapiens
-
IC50: 35 nM
0.00369
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00743
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00169
3-acetyl-5,8-dibromo-2-[(4-bromophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00359
3-acetyl-5,8-dibromo-2-[(4-bromophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00317
3-acetyl-5,8-dichloro-2-[(2,4-dichlorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00399
3-acetyl-5,8-dichloro-2-[(2,4-dichlorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00316
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00464
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00239
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00373
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00353
3-acetyl-8-bromo-5-chloro-2-[(4-chlorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00994
3-acetyl-8-bromo-5-chloro-2-[(4-chlorophenyl)amino]quinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.000277
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00028
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00306
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.00456
3-acetyl-8-chloro-2-[(4-chlorophenyl)amino]-6-nitroquinolin-4(1H)-one
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, pH 7.5, at 25°C
0.00808
3-acetyl-8-chloro-2-[(4-chlorophenyl)amino]-6-nitroquinolin-4(1H)-one
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.000199
MDL28170
Homo sapiens
-
using dye-Gln-Gln-Gln-Glu-Val-Tyr-Gly-Met-Met-Pro-Arg-Asp-pSer-Ala as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
0.0002
MDL28170
Homo sapiens
-
using [2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 as substrate, in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 5 mM beta-mercaptoethanol, at 25°C, pH 7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.3
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
-
pH 6.5: about 35% of maximal activity, pH 8.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
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
-
644001, 644004, 667778, 677829, 677835, 679684, 680392, 680394, 696290, 709798, 717053, 731906, 731990
-
-
brenda
Charolaise, Hereford, Limousine, Simmental, Polish Red, and Fresian breeds
-
-
brenda
fragment; Spanish maternal beef breeds Retinta, Morucha, and Avilena Negra-Iberica
UniProt
brenda
-
643975, 643976, 643978, 643985, 643987, 643989, 643991, 643992, 643993, 643997, 644003, 663588, 667136, 667872, 667939, 669201, 669300, 677501, 677919, 678348, 678537, 678542, 679230, 679254, 679823, 680421, 680713, 680913, 681012, 681694, 690381
-
-
brenda
-
707053, 707364, 707373, 707531, 707532, 707560, 707564, 707874, 708028, 708051, 708194, 708257, 708270, 708416, 708490, 708643, 708745, 708761, 708806, 708901, 709049, 709406, 709438, 709599, 709600, 709640, 709641, 709652, 709659, 709720, 710069, 710164, 710561, 717187, 718111, 731892, 732676, 732787
-
-
brenda
-
669371, 678984, 680185, 690381, 695462, 697162, 707065, 707082, 707296, 708018, 708717, 709015, 709152, 709681, 709857, 709967, 710042, 717198, 717201, 717453, 718096, 731222, 731339, 731364, 732688
-
-
brenda
-
643977, 643979, 643983, 643984, 643987, 643996, 643998, 644000, 644002, 644005, 644006, 670009, 677455, 679438, 680913, 690381, 696451, 699654, 700426, 707281, 707559, 707936, 708015, 708016, 708194, 708434, 708435, 708437, 708438, 708781, 709624, 709712, 710087, 710409, 731339, 731364, 731589
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activation of mu-calpain in platelets from patients with type 2 diabetes mellitus
brenda
-
from patients with recurrent miscarriage and healthy women with informed consent
brenda
-
rheumatic synovial cell line. mu-calpain, regulates MMP-3 release by rheumatic synovial cells, in addition to exerting its own degradative action on cartilage
brenda
-
first molar of foetal ICR mice from embryonic day 14 to postnatal day 7
brenda
the large catalytic subunits of calpains 1 and the small regulatory subunit common to calpains 1 and 2 are weakly expressed in the parotid gland, sublingual gland, and submandibular gland at similar levels in males and females
brenda
-
NO-induced motility in osteoclasts requires regulated Ca2+ release, which activates mu-calpain. This occurs via the inositol (1,4,5)-trisphosphate receptor 1
brenda
-
elevated levels of calpain-1 in glaucomatous trabecular meshwork. However, calpain activity in glaucomatous trabecular meshwork is only about 50% of that in controls. Modification by iso-levuglandins renders calpain-1 inactive
brenda
the large catalytic subunits of calpains 1 and the small regulatory subunit common to calpains 1 and 2 are weakly expressed in the parotid gland, sublingual gland, and submandibular gland at similar levels in males and females
brenda
additional information
-
protein phosphatase 2A functions as a physiological calpain phosphatase to directly dephosphorylate mu-calpain, which leads to decreased calpain activity and suppression of migration and invasion of human lung cancer cells
brenda
-
white matter from patients with MS and Parkinsons and Alzheimers diseases and white matter from normal control
brenda
-
white matter of young, middle aged and old monkeys, age-dependent myelin degeneration and proteolysis of oligodendrocyte proteins is associated with the activation of calpain-1
brenda
-
white matter of young, middle aged and old monkeys, age-dependent myelin degeneration and proteolysis of oligodendrocyte proteins is associated with the activation of calpain-1
brenda
-
-
brenda
-
prednisolone suppresses ischemia-reperfusion injury of the rat liver. Its cytoprotective effect is partial, but is closely associated with inhibition of activation of mu-calpain and suppression of IL-beta and TNF-alphatranscription as well as with improved survival rate
brenda
-
small interfering RNAs-mediate knockdown of mu-calpain expression in MCF-7 cells that do not express m-calpain leads to a reduction of cell migration
brenda
-
musculus longissimus thoracis et lumborum, loss of activity during postmortem aging
brenda
-
mu-calpain rapidly loses their activity during postmortem storage, so that proteolytic activity of mu-calpain is nearly zero after 3 d postmortem, even when assayed at pH 7.5 and 25°C
brenda
-
musculus longissimus thoracis et lumborum, loss of activity during postmortem aging
brenda
-
calpains are autolyzed in the early stage of skeletal muscle atrophy. Calpain 1 autolysis occurs without any modification in the total amount. Calpain autolysis is only seen in the slow soleus muscle, while the fast plantaris muscle is not affected. Calpain autolysis and caspase 3 activation found in the soleus muscle could explain a more atrophied condition of this muscle compared with the plantaris muscle
brenda
-
autolysis of both mu-calpain and calpain-3 is tightly regulated by Ca2+ concentration in skeletal muscle across a range close to but evidently above that reached during normal activity
brenda
-
excentric exercise produces little autolytic activation of mu-calapin
brenda
-
in skeletal muscle, mu-calpain is a freely diffusible protein
brenda
-
localisation in the Z-band and under the plasma membrane
brenda
-
in skeletal muscle, mu-calpain is a freely diffusible protein
brenda
the large catalytic subunits of calpains 1 and the small regulatory subunit common to calpains 1 and 2 are weakly expressed in the parotid gland, sublingual gland, and submandibular gland at similar levels in males and females
brenda
additional information
-
Plasmodium falciparum-calpain is expressed in all erythrocytic stages, the expression of Plasmodium falciparum-calpain is increased much more when the late ring matures into the early trophozoite
brenda
additional information
-
Plasmodium falciparum-calpain is expressed in all erythrocytic stages, the expression of Plasmodium falciparum-calpain is increased much more when the late ring matures into the early trophozoite
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
calpain-1 is relocated and translocated from cytoplasm to plasma membrane during capacitation
brenda
-
membrane-binding of mu-calpain is Ca2+-dependent. Membrane binding of mu-calpain is due to the exposed hydrophobic surface of the active site conformation and does not reduce the Ca2+ requirement for activation
brenda
-
association between l-calpain and calpastatin in the mitochondria
brenda
-
mu-calpain is present in the inner mitochondrial membrane, but not in the outer mitochondrial membrane or in the inter membrane space or in the matrix of the mitochondria. mu-Calpain-calpastatin is associated in the inner mitochondrial membrane. mu-Calpain is integrally and calpastatin is peripherally embedded to the outer surface of inner mitochondrial membrane
brenda
-
both calpain 1 and calpain small subunit 1, which together form mu-calpain, are present in the mitochondrial intermembrane space. The N-terminus of calpain 1 is not processed following mitochondrial import, but is removed by autolysis following calpain activation. Calpain small subunit 1 is not directly imported into mitochondria, but is imported in the presence of calpain 1. The presence of a mitochondrial targeting sequence in the N-terminal region of calpain 1 is consistent with the localization of mu-calpain to the mitochondrial intermembrane space
brenda
mitochondrial calpain 1 is located within the intermembrane space and mitochondrial matrix
brenda
-
both calpain 1 and calpain small subunit 1, which together form mu-calpain, are present in the mitochondrial intermembrane space. The N-terminus of calpain 1 is not processed following mitochondrial import, but is removed by autolysis following calpain activation. Calpain small subunit 1 is not directly imported into mitochondria, but is imported in the presence of calpain 1. The presence of a mitochondrial targeting sequence in the N-terminal region of calpain 1 is consistent with the localization of mu-calpain to the mitochondrial intermembrane space
brenda
-
a pool of micro-calpain is localized to the mitochondrial intermembrane space
brenda
-
mu-calpain, including both the large and small subunits is present in the mitochondrial intermembrane space
brenda
-
calpain-1 normally localizes to the interphase nuclei and chromatin
brenda
-
calpain-1 is relocated and translocated from cytoplasm to plasma membrane during capacitation
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
calpain inhibition does not protect endothelial cells during cold storage
malfunction
-
calpain inhibition prevents NMDA-induced AIF truncation and nuclear translocation in neurons
malfunction
-
calpain-1 overactivation in mitochondrial-deficient cells promotes caspase-3 activation, calpain inhibition decreases alpha-synuclein oligomerization
malfunction
-
immunodepletion or inhibition of calpain-1 in hypotonically lysed and resealed erythrocytes prevents the escape of Plasmodium falciparum parasites. Similarly, efficient egress of Tooplasma gondii from mammalian fibroblasts is blocked by either small interfering RNA-mediated suppression or genetic deletion of calpain activity
malfunction
-
in utero knockdown of calpain by shRNA rescues defective cortical layering in heterozygous Lis1+/? mice
malfunction
-
inhibition of micro-calpain not only significantly reduces caspase-9/-3 activities but also completely blocks apoptosis-inducing factor redistribution
malfunction
-
knocking down mu-calpain by siRNA in FA-A cells restores levels of alphaII-spectrin to normal and reverses a number of the cellular deficiencies in these cells. siRNA knockdown of mu-Calpain in FA-A cells leads to increased cell viability and formation of nuclear foci after damage with a DNA interstrand cross-linking agent
malfunction
-
engineered cleavage of Rad21 at the calpain-cleavable site without activation of calpain-1 can lead to a loss of sister chromatid cohesion
malfunction
-
expression levels of galectin-3 are unchanged when calpain 1 is silenced
malfunction
-
calpain inhibition favors differentiation of neuronal stem cells. Calpain 1 silencing results in increased levels of both neuronal and glial markers, beta-III tubulin and glial fibrillary acidic protein
malfunction
-
suppression of calpain 1 significantly reduces cell viability in cell proliferation when compared with control cells. Suppression of calpain 1 results in an increase in the expressions of apoptotic caspases such as caspase-3, caspase-6, caspase-7, caspase-8, and caspase-9, as well as heat-shock protein systems and leads to the upregulation of other apoptosis and DNA damage-regulating genes whilst at the same time downregulating proliferation, migration, and differentiation-regulating genes
malfunction
-
the knockdown of calpain 1 increases cell adhesion (by 36% after 30 min), enhances migration (by 46% after 12 h), and stabilizes late-stage cord formation on Matrigel by increasing cord length compared to the control human lymphatic microvascular dermal-derived endothelial cells
metabolism
-
calpain 1 is involved in the degradation of endothelial nitric oxide synthase and heat shock protein 90 and the phosphorylation of endothelial nitric oxide synthase
metabolism
calpain-1 regulates platelet function in a humanized mouse model of sickle cell disease
physiological function
-
activation of micro-calpain plays an essential role in regulating both caspase-dependent and apoptosis-inducing factor-mediated caspase-independent apoptotic pathways in cisplatin-induced apoptosis
physiological function
-
calcium-dependent plasma membrane repair requires mu-calpain
physiological function
-
calpain 1 activation contributes to HIF-2alpha degradation by IH
physiological function
-
calpain activation is required for homocysteine-mediated hepatic degradation of inhibitor Ikappa B alpha
physiological function
-
calpain activation precedes caspase-12 activation in the Ca2+-mediated apoptotic cascade and, thus, may be necessary for caspase-12 activation
physiological function
-
calpain degrades myofibrillar protein under post-mortem condition and is the primary enzyme in the postmortem tenderization process
physiological function
-
calpain I is not required for mitochondrial apoptosis-inducing factor release in poly(ADP-ribose) polymerase-1-dependent cell death
physiological function
-
calpain regulates trastuzumab sensitivity and survival, and the deregulation of the activation of calpain promotes trastuzumab resistance, trastuzumab-resistant cells require calpain activity for survival and activation of AKT1
physiological function
-
calpain-1 activation induces apoptosis through down-regulation of the Na+/K+ ATPase activity in high glucose-stimulated cardiomyocytes and in vivo hyperglycaemic hearts. High glucose-induced calpain-1 activation is mediated through the NADPH oxidase-dependent pathway and associated with activation of L-type calcium channels and ryanodine receptors
physiological function
-
calpain-1 induces apoptosis in pulmonary microvascular endothelial cells under septic conditions
physiological function
-
calpain-I activity colocalizes with apoptotic cell death
physiological function
dramatic muscle growth during the neonatal period may be partially controlled by down-regulated calpain-calpastatin system
physiological function
-
gp91phox-NADPH oxidase-mediated calpain-1 activation induces caspase-3 activation and tumour necrosis factor-alpha expression in cardiomyocytes during lipopolysaccaride stimulation
physiological function
-
micro-calpain is a key signal released from 1-methyl-4-phenylpyridinium-damaged neurons, causing selective dopaminergic neuron death through activation of microglial NADPH oxidase and superoxide production. Extracellular micro-calpain activates microglia
physiological function
-
mitochondrial mu-calpain is an initiator of the apoptosis-inducing factor-induced cell death signaling pathway. Mitochondrial calpain plays important roles both in caspase-dependent and -independent pathways in cell death phenomena. Mu-calpain can act as a direct activator of apoptosis-inducing factor release in neuronal cultures challenged with oxygen-glucose deprivation
physiological function
-
mu-calpain is responsible for Ca2+-induced disruption of excitation-contraction coupling
physiological function
-
mu-calpain is specifically recruited into the NMDA receptor-neuronal nitric oxide synthase-heat shock protein 90 complex following calcium loading
physiological function
-
mu-calpain plays a role in membrane repair and a protective role in skeletal muscle
physiological function
-
mu-calpain plays a role in membrane repair and a protective role in skeletal muscle
physiological function
mu-calpain plays an important role in the postmortem tenderization process of meat
physiological function
-
mu-calpain up-regulates alpha- and beta-actin in alveolar rhabdomyosarcoma cells
physiological function
-
calpain-1 inhibits the acrosome reaction and alters the plasma membrane-associated cytoskeleton in spermatozoa
physiological function
-
exogenous calcium treatment induces a calpain-dependent decrease of mitochondrial apoptosis inducing factor content in isolated mouse heart mitochondria
physiological function
-
mu-calpain proteasome-dependent I-kappaBalpha polymer degradation may contribute to cancer progression through constitutive nulear factor-kappaB activation
physiological function
-
Rad21 cleavage by calpain-1 promotes separation of sister chromatid arms
physiological function
-
calpain 1 plays a role in repressing differentiation, thus maintaining a proliferative neuronal stem cell pool
physiological function
-
calpain is involved in lysosomal membrane permeabilization
physiological function
-
calpain is involved in lysosomal membrane permeabilization
physiological function
-
calpain-1 induces endoplasmic reticulum stress and c-Jun N-terminal protein kinase1/2 activation, thereby mediating apoptosis in cardiomyocytes following hypoxia/reoxygenation. Up-regulation of calpain-1 induces increases in caspase-3 activation and DNA fragmentation, indicative of apoptosis
physiological function
-
calpain-1 induces endoplasmic reticulum stress and c-Jun N-terminal protein kinase1/2 activation, thereby mediating apoptosis in cardiomyocytes following hypoxia/reoxygenation. Up-regulation of calpain-1 induces increases in caspase-3 activation and DNA fragmentation, indicative of apoptosis
physiological function
-
mu-calpain is involved in the postmortem proteolysis of gizzard smooth muscle
physiological function
-
mu-calpain is involved in the postmortem proteolysis of gizzard smooth muscle
physiological function
-
neuronal death has a direct relationship with calpain I activity. Calpain I plays an important role in neuronal damage during status epilepticus
physiological function
-
the enzyme plays a role in the early phase and during progression of amyotrophic lateral sclerosis
physiological function
-
the enzyme plays key roles in regulation of cell proliferation and survival of of bovine skeletal satellite cells
physiological function
activated mitochondrial calpain 1 within intermembrane space cleaves apoptosis inducing factor (AIF), whereas the activated mitochondrial calpain 1 within the matrix cleaves complex I subunits and metabolic enzymes
physiological function
calpain 1 activity within neutrophils is necessary for them to undergo efficient phagocytosis
physiological function
calpain-1 accumulation in mitochondria disrupts ATP synthase and induces ROS generation, which promotes diabetic cardiomyopathy
physiological function
calpain-1 and calpain-2 play opposite functions in both synaptic plasticity/learning and memory and neuroprotection/neurodegeneration. Calpain-1 activation is necessary for certain forms of synaptic plasticity and learning and memory, while calpain-2 activation during a brief consolidation period limits the extent of plasticity/learning. Calpain-1 is neuroprotective, while calpain-2 is neurodegenerative
physiological function
calpain-1 and calpain-2 play opposite roles in retinal ganglion cell death induced by acute intraocular pressure elevation. Calpain-1 activity supports survival of retinal ganglion cell after intraocular pressure elevation. Calpain-2 activity promotes cell death of retinal ganglion cells after intraocular pressure elevation
physiological function
dynamin-like protein 1 (DLP1) is the key mitochondrial fission GTPase. It is a substrate of calpain which produced specific N-terminal DLP1 cleavage fragments. DLP1 is a physiological and Alzheimer's disease-relevant pathophysiological substrate of calpain in cells and in the brain. Calpain activation could contribute to reduced DLP1 levels and mitochondrial dynamics abnormalities and mitochondrial dysfunction in Alzheimer's disease
Show AA Sequence and Transmembrane Helices (1207 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
29000
32000
74000
75000
76000
80000
83000
29000
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1 * 83000 + 1 * 29000, an isolated 70000 Da calpain I, or monomeric artifact is also detected, SDS-PAGE
83000
-
1 * 83000 + 1 * 29000, an isolated 70000 Da calpain I, or monomeric artifact is also detected, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
additional information
dimer
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1 * 83000 + 1 * 29000, an isolated 70000 Da calpain I, or monomeric artifact is also detected, SDS-PAGE
additional information
-
EC 3.4.22.52 is not derived by the autolysis of EC 3.4.22.53, but it is an independent species
additional information
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Ca2+ causes autoproteolytic conversion of the native 80000 Da subunit into the active 75000 Da subunit
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
proteolytic modification
phosphoprotein
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protein phosphatase 2A functions as a physiological calpain phosphatase to directly dephosphorylate mu-calpain, which leads to decreased calpain activity and suppression of migration and invasion of human lung cancer cells
phosphoprotein
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brain-derived neurotrophic factor does not stimulate mu-calpain serine phosphorylation
proteolytic modification
-
autolysis of both mu-calpain and calpain-3 is tightly regulated by Ca2+ concentration in skeletal muscle across a range close to but evidently above that reached during normal activity
proteolytic modification
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calpains are autolyzed in the early stage of skeletal muscle atrophy. This autolysis is specific to the particulate fraction for calpain 1 and to the soluble fraction for calpain 2, indicating specific microlocalization of calpain autolysis regulation. Calpain 1 autolysis occurs without any modification in the total amount. Calpain autolysis is only seen in the slow soleus muscle, while the fast plantaris muscle is not affected. Calpain autolysis and caspase 3 activation found in the soleus muscle could explain a more atrophied condition of this muscle compared with the plantaris muscle
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the mu-calpain single nucleotide polymorphisms C80T, C302G, G310A, C445T, and A524C are associated with tenderness in beef cattle
additional information
the mu-calpain single nucleotide polymorphisms C80T, C302G, G310A, C445T, and A524C are associated with tenderness in beef cattle
additional information
the mu-calpain single nucleotide polymorphisms C80T, C302G, G310A, C445T, and A524C are associated with tenderness in beef cattle
additional information
-
the mu-calpain single nucleotide polymorphisms C80T, C302G, G310A, C445T, and A524C are associated with tenderness in beef cattle
additional information
-
polymorphisms in the calpain 1 gene influence meat quality in carcass trait
additional information
-
the mutant enzyme L-muyCANPDELTA3 requires 0.4-0.53 mM of Ca2+ compared to 0.06 mM for the native enzyme, bacterially expressed mutant enzyme L-muyCANPDELTA3. A chimeric form composed of domains I-III of muCANP and domain IV of calpain II is also expressed in Sf9 cells. This mutant requires less Ca2+, 0.05 mM, than the native erythrocyte enzyme and has the highest specific activity of all calpains tested. All recombinant proteins are active as monomers in polyethylene glycol-containing buffers. The in vitro association with the regulatory subunit enhances only slightly the maximal velocity and the Ca2+ dependence of the expressed proteins
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the 70000 Da monomeric calpain I is less pH stable than the parent heterodimeric calpain I
643981
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58
additional information
-
the 70000 Da monomeric calpain I is much less heat stable than the parent heterodimeric calpain I
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
m-calpain loses 50-55% of its proteolytic activity within 5 min during incubation at pH 7.5 in 300 mM or high salt and at a slower rat in 100 mM salt. This loss of activity is not reversed by dialysis for 18 h against a low-ionic-strength buffer at pH 7.5. Proteolytic activity of the unautolyzed calpains is not affected by incubation for 45 min at ionic strength up to 1000 mM. Ionic strengths of 100 mM or above cause dissociation of the two subunits of autolyzed calpains. The dissociated large subunits aggregate to form dimers and trimers, which are proteolytically inactive
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography, calmodulin-like domain of the catalytic subunit expressed in E. coli
-
partial
single-step purification of calpain-1, calpain-2, and calpastatin using anion-exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 289 bp fragment for mu-calpain is cloned into the EcoRV site of pBluescript II KS+ vector
cloning of the 21000 Da small subunit and expression in Escherichia coli BL384
-
complete amino acid sequence of the large subunit is deduced from its cDNA sequence
large catalytic subunit and two of its mutants are expressed in Escherichia coli using the baculovirus Sf9 system, the L-muCANPDELTA3 mutant lacks domain III, mutant L-muCANPDELTA4 lacks the calmodulin-like domain IV. In Sf9 cells co-expression of the inhibitor calpastatin is necessary to prevent autolysis of the L-muCANP subunit, whereas coexpression of the regulatory subunit enhances it. Only very low levels of mRNA of the truncated form L-muCANPDELTA4 are found in bacmid-transfectred Sf9 cells, and it proves impossible to isolate this mutant using the baculovirus expression system
-
the cDNA fragments corresponding to the domains with four consecutive E-F hand structures in the large and small subunits are inserted into an expression vector, pUC8 or pUC17. The resulting plasmids are used to transform Escherichia coli and isopropyl-1-thio-beta-D-galactoside-inducible expression is performed
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after ageing of large cuts of beef loin in vacuum or high oxygen modified atmosphere mu-calpain activity declines below the detection limit in all ageing systems
-
although the levels of the calpain I isoform are higher in the soluble and insoluble fractions of tir- and wild type enteropathogenic Escherichia coli (E2348/69 O127:H6)-infected cells, their levels are not significantly different to the TTSS-negative control
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an increase in the activity of calpain-1 takes place at an early stage of amyotrophic lateral sclerosis
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at 24 h after status epilepticus, activity of calpain I increases in the hippocampus
-
at 24 h postmortem the activity of the native mu-calpain decreases. A faster decrease in pH results in reduced level of mu-calpain activity and increased autolysis of the enzyme
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calpain 1 activity is increased 2.5fold in FA-A, FA-D2, and FA-F cells as compared to normal cells and 3.5fold in FA-C and FA-G cells compared to normal cells
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calpain 1 expression levels are high in self-renewing neuronal stem cells and decrease with differentiation
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calpain 1 protein and mRNA levels are low at early developmental time points and increase dramatically by postnatal day 30. Immunoreactivity of the 80 kDa calpain 1 increases 75% from embryonic day 18 to postnatal day 90, with the increase being most rapid between postnatal day 10 and postnatal day 20 in rat brain
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calpain activity in liver of heterozygous cystathionine beta synthase-deficient mice shows a 30% increase compared to wild type mice
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calpain activity increases in cells exposed to intermittent hypoxia 60 and 0.01 mM 1,2-bis(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetra(acetoxymethyl) ester prevents this effect
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calpain-1 protein and activity in mitochondria are elevated in diabetic mouse hearts
calpain1 mRNA is increased in the all enamel epithelia between embryonic day 18 and postnatal day 1, calpastatin mRNA expression increases in the ameloblasts from postnatal days 1 to 7
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cell infection with Ad-capn1 and significantly elevates the protein level of calpain-1
cold storage (at 4°C) induces a time dependent up-regulation of calpain 1, reflected by an increase in the autoproteolytic cleavage of calpain 1, which can be prevented by addition of EDTA or dopamine (0.025 mM) pretreatment
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compared to control cybrids, Parkonsins disease cybrids reveal a significant increase in calpain activity
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compared with 5-month-old mice, there is no change in calpain 1 in 16-month-old mice
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high glucose (33 mM) induces calpain-1 activation in cardiomyocytes. Gp91phox-NADPH oxidase contributes to calpain-1 activation in high glucose-induced cardiomyocytes
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in comparison to the sham operation group, the activity of calpain I is 1.1fold decreased in the calpain inhibitor group (N-acetyl-L-Leu-L-Leu-L-Met (1.0 mg/kg/day))
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in comparison to the sham operation group, the activity of calpain I is significantly increased (2.3fold) in the control atrial fibrillation group
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in cultured pulmonary microvascular endothelial cells, incubation with septic plasma stimulates calpain activation. Reactive oxygen species produced from NADPH oxidase stimulates calpain-1 activation
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in healthy mice, calpeptin treatment causes a significant increase in micro-calpain
-
in mice with myocardial infarction, calpeptin treatment causes a significant decrease in micro-calpain level
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inner ear cell death due to apoptosis occurs in a time-dependent manner with concomitant up-regulation of calpain-I expression
-
ionomycin and thapsigragin, which elevate [Ca2+], activate calpains in cells exposed to normoxia
-
listeriolysin O-dependent bacterial entry into the cytoplasm is required for calpain activation and interleukin-1 alpha secretion in macrophages infected with Listeria monocytogenes
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low nutritional level diet treatment increases mRNA level of micro-calpain in skeletal muscle
-
mitochondrial mu-calpain activity is increased by 160% during ischemia-reperfusion compared to time control
-
mu-calpain activity decreases by about 37% immediately and 2 h after acute-exhaustive exercise
-
mu-calpain expression levels are unchanged by laminar shear flow or disturbed shear flow stimulus
-
mu-calpain is not activated immediately following sprint, endurance or eccentric exercise. mu-Calpain is not activated 24 h after a single bout of eccentric exercise
Protein Never in Mitosis Gene A Interacting-1 reduces calpain activity and slows the degradation of COX-2 in MAEC cells
-
the steady-state mRNA level of calpain 1A decreases by 2-4fold at the age of 4 to 6 days compared to 1-day-old piglets. Expressions of calpain 1A is negatively correlated with birth weight and fractional rate of growth, decreased levels of calpain 1A expressions over development in neonatal pigs are associated with high protein accumulations
there are no significant differences on the expressions of calpain-1 at the levels of mRNA and protein in patients with and without stress urinary incontinence
-
there is no age-dependent change in calpain 1 protein expression in control or caloric-restricted rats. Liver samples taken from control rats at 4, 9, and 24 months and from caloric-restricted rats at 24 months do not exhibit any changes in calpain 1 protein expression
-
there is no age-related change in calpain 1 protein expression in human female or male kidney samples. In the human kidney, there is no age-related change in calpain 1 mRNA expression
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treatment with 50 mg/kg 7-nitroindozale shows significant suppression of the activity of mu-calpain in brain cortex (penumbra), however, it has no significant effect on the mu-calpain activity in core (striatum and overlying cortex)
-
cell infection with Ad-capn1 and significantly elevates the protein level of calpain-1
-
cell infection with Ad-capn1 and significantly elevates the protein level of calpain-1
-
mu-calpain is not activated immediately following sprint, endurance or eccentric exercise. mu-Calpain is not activated 24 h after a single bout of eccentric exercise
-
mu-calpain is not activated immediately following sprint, endurance or eccentric exercise. mu-Calpain is not activated 24 h after a single bout of eccentric exercise
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
-
markers developed at the CAST and CAPN1 genes are suitable for use in identifying animals with the genetic potential to produce meat that is more tender
medicine
medicine
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protein phosphatase 2A functions as a physiological calpain phosphatase to directly dephosphorylate mu-calpain, which leads to decreased calpain activity and suppression of migration and invasion of human lung cancer cells. Therapeutic activation of protein phosphatase 2A to dephosphorylate calpain by enhancing ceramide production may have clinical relevance for the treatment of cancer metastasis
medicine
-
role for the mu-calpain isoform in the hypermeability of the diabetic endothelium. mu-calpain is the molecular target of the endothelial protective action of pharmacological calpain inhibition in vivo
medicine
-
calpain and calpain inhibition is a therapeutic tool in Parkinsons disease
medicine
-
calpain inhibition attenuates endotoxin-induced diaphragm weakness, suggesting that such inhibitors may be a potential treatment to improve respiratory function in infected patients
medicine
-
calpain-1 activation is important in the development of diabetic cardiomyopathy and thus represents a potential therapeutic target for diabetic heart diseases
medicine
-
manipulating calpain activity by calpain inhibitor SNJ-1945 is a therapy for management of pathological angiogenesis, such as that occurring in proliferative retinopathy and age-related macular degeneration with neovascularization
medicine
-
mu-calpain is a marker of tumor aggressiveness and is apotential target for limiting development of rhabdomyosarcoma tumor as well as their metastatic behavior
medicine
-
the inhibition of calpain is a potential therapeutic intervention for lissencephaly
medicine
calpain-1 regulates platelet hyperactivity in sickle mice, and may offer a viable pharmacological target to reduce platelet hyperactivity in sickle cell disease
medicine
inhibition of the mitochondrial calpain 1 could be a potential strategy to decrease cardiac injury during ischemia-reperfusion
medicine
since calpain inhibition prevents diabetes-induced endothelial dysfunction in mesenteric arteries. Calpains represent an interesting therapeutic target for the prevention of cardiovascular complication of diabetes
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Release 2023.1 (January 2023)
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