Information on EC 3.4.22.52 - calpain-1

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
3.4.22.52
-
RECOMMENDED NAME
GeneOntology No.
calpain-1
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
broad endopeptidase specificity
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase; peptides, endopeptidase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
calcium-activated neutral protease I
-
-
-
-
calpain 1
-
-
-
-
calpain 1
-
-
calpain 1
P07384
-
calpain 1
-
-
calpain 1
-
-
calpain 1A
P35750
calpain 1 catalytic subunit
calpain I
-
-
-
-
calpain I
-
-
calpain small subunit
-
-
calpain-1
-
-
calpain-1
-
-
calpain-1
-
-
calpain-1 (micro-form)
-
-
calpain-I
-
-
calpain-I
-
-
calpain1
-
-
calpain1
-
-
CAPN1
C6ERB9, C6ERC0, C6ERC1
-
CAPN1
-
-
CAPN1
-
-
CAPN1
-
-
CAPN1 g.p. (Homo sapiens)
-
-
-
-
CAPNS1
-
-
cysteine protease
-
-
EC 3.4.22.17
-
formerly
m-CANP
-
-
micro-calpain
-
-
-
-
micro-calpain
-
-
micro-calpain
-
-
micro-calpain
-
-
mito-mu-calpain
-
-
mu-calpain
-
-
-
-
mu-calpain
C6ERB9, C6ERC0, C6ERC1
-
mu-calpain
-
-
mu-calpain
-
-
mu-calpain
-
-
mu-calpain
-
isoform
muCANP
-
-
-
-
muI-II
-
calpain 1 protease core
CAS REGISTRY NUMBER
COMMENTARY
689772-75-6
-
78990-62-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Charolaise, Hereford, Limousine, Simmental, Polish Red, and Fresian breeds
-
-
Manually annotated by BRENDA team
fragment; Spanish maternal beef breeds Retinta, Morucha, and Avilena Negra-Iberica
UniProt
Manually annotated by BRENDA team
lamb
-
-
Manually annotated by BRENDA team
calpain-1 catalytic subunit
SwissProt
Manually annotated by BRENDA team
strain FCR-3
-
-
Manually annotated by BRENDA team
Plasmodium falciparum FCR-3
strain FCR-3
-
-
Manually annotated by BRENDA team
Fisher 344 x Brown Norway, male, 8-month old or 30-month old
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
calpain 1 catalytic subunit
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
calpain inhibition prevents NMDA-induced AIF truncation and nuclear translocation in neurons
malfunction
-
inhibition of micro-calpain not only significantly reduces caspase-9/-3 activities but also completely blocks apoptosis-inducing factor redistribution
malfunction
-
calpain inhibition does not protect endothelial cells during cold storage
malfunction
-
in utero knockdown of calpain by shRNA rescues defective cortical layering in heterozygous Lis1+/? mice
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
-
expression levels of galectin-3 are unchanged when calpain 1 is silenced
malfunction
-
engineered cleavage of Rad21 at the calpain-cleavable site without activation of calpain-1 can lead to a loss of sister chromatid cohesion
physiological function
-
mu-calpain is responsible for Ca2+-induced disruption of excitation-contraction coupling
physiological function
C6ERB9, C6ERC0, C6ERC1
mu-calpain plays an important role in the postmortem tenderization process of meat; mu-calpain plays an important role in the postmortem tenderization process of meat; mu-calpain plays an important role in the postmortem tenderization process of meat
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
-
calpain activation precedes caspase-12 activation in the Ca2+-mediated apoptotic cascade and, thus, may be necessary for caspase-12 activation
physiological function
-
calcium-dependent plasma membrane repair requires mu-calpain
physiological function
-
calpain-I activity colocalizes with apoptotic cell death
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
-
gp91phox-NADPH oxidase-mediated calpain-1 activation induces caspase-3 activation and tumour necrosis factor-alpha expression in cardiomyocytes during lipopolysaccaride stimulation
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
-
mu-calpain plays a role in membrane repair and a protective role in skeletal muscle
physiological function
P35750
dramatic muscle growth during the neonatal period may be partially controlled by down-regulated calpain-calpastatin system
physiological function
-
mu-calpain up-regulates alpha- and beta-actin in alveolar rhabdomyosarcoma cells
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
-
mu-calpain is specifically recruited into the NMDA receptor-neuronal nitric oxide synthase-heat shock protein 90 complex following calcium loading
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-1 induces apoptosis in pulmonary microvascular endothelial cells under septic conditions
physiological function
-
calpain degrades myofibrillar protein under post-mortem condition and is the primary enzyme in the postmortem tenderization process
physiological function
-
calpain activation is required for homocysteine-mediated hepatic degradation of inhibitor Ikappa B alpha
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 contributes to HIF-2alpha degradation by IH
physiological function
-
mu-calpain proteasome-dependent I-kappaBalpha polymer degradation may contribute to cancer progression through constitutive nulear factor-kappaB activation
physiological function
-
exogenous calcium treatment induces a calpain-dependent decrease of mitochondrial apoptosis inducing factor content in isolated mouse heart mitochondria
physiological function
-
calpain-I is involved in kanamycin-induced ototoxicity
physiological function
-
Rad21 cleavage by calpain-1 promotes separation of sister chromatid arms
physiological function
-
calpain-1 inhibits the acrosome reaction and alters the plasma membrane-associated cytoskeleton in spermatozoa
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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)
show the reaction diagram
-
-
-
-
?
(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
show the reaction diagram
-
-
-
-
?
(EDANS)-EALFAERK-(DABCYL) + H2O
(EDANS)-EA + LFAERK-(DABCYL)
show the reaction diagram
-
about 30% cleavage preference
-
-
?
(EDANS)-EPLFAARK-(DABCYL) + H2O
(EDANS)-EPLFA + ARK-(DABCYL)
show the reaction diagram
-
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)
show the reaction diagram
-
about 40% cleavage preference
-
-
?
(EDANS)-EPLFGERK-(DABCYL) + H2O
(EDANS)-EPLF + GERK-(DABCYL)
show the reaction diagram
-
less than 20% cleavage preference
-
-
?
(EDANS)-EPLFMERK-(DABCYL) + H2O
(EDANS)-EPLF + MERK-(DABCYL)
show the reaction diagram
-
the peptide sequence PLFMER is rapidly cleaved by the calpain 1 core at the F-M bond with about 45% cleavage preference
-
-
?
2',3'-cyclic nucleotide 3'-phosphodiesterase + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-EVYGMMY(3-NO2)-OH + H2O
2-aminobenzoyl-EVY + GMMY(3-NO2)-OH
show the reaction diagram
-
-
-
-
?
4,4-difluoro-5,7-dimethyl-4-bora-31,4a-diaza-s-indacene-3-propioyl-labeled casein + H2O
?
show the reaction diagram
-
-
-
-
?
5-([4,6-dichlorotriazin-2-yl]amino)fluorescin-labeled microtubule-associated protein 2 + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
acetyl-Leu-Leu-Tyr-7-amido-4-trifluoromethyl coumarin + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-LLY-7-amido-4-fluoromethylcoumarin + H2O
acetyl-LLY + 7-amino-4-fluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
AIF + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-actinin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-II-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-II-spectrin + H2O
?
show the reaction diagram
-
-
calpain-specific spectrin cleaved products
-
?
alpha-spectrin
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
-
mu-calpain is neuroprotective in the earyl 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
-
-
?
alpha-spectrin II + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-subunit of fodrin + H2O
150000 Da fragment + ?
show the reaction diagram
-
-
-
?
alpha-synuclein + H2O
145000 DA fragment + 150 Da fragment + ?
show the reaction diagram
-
-
-
-
?
alphaII-spectrin + H2O
?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
-
-
?
apoptosis-inducing factor + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
calpain-mediated truncation of apoptosis-inducing factor is contingent upon poly(ADP-ribose) polymerase-1 activity
-
-
?
apoptosis-inducing factor + H2O
?
show the reaction diagram
-
micro-calpain mediates the truncation and release of apoptosis-inducing factor from mitochondria following cisplatin treatment
-
-
?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
show the reaction diagram
-
-
-
-
?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
show the reaction diagram
-
mitochondrial micro-calpain is the protease responsible for processing apoptosis-inducing factor prior to its release
-
-
?
beta-integrin + H2O
?
show the reaction diagram
-
-
-
-
?
BH3-only Bcl2 interacting domain + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
10 microM, 20 min, 37 C, with or without magnetic bead stimulation
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
P35750
-
-
-
?
caspase-7 + H2O
?
show the reaction diagram
-
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
-
-
?
collapsin response mediator protein 1 + H2O
?
show the reaction diagram
-
-
-
-
?
collapsin response mediator protein 2 + H2O
?
show the reaction diagram
-
-
-
-
?
collapsin response mediator protein 3 + H2O
?
show the reaction diagram
-
-
-
-
?
collapsin response mediator protein 4 + H2O
?
show the reaction diagram
-
-
-
-
?
COX-2 + H2O
?
show the reaction diagram
-
-
-
-
?
cyclin dependent kinase-5 + H2O
p25-CDK5
show the reaction diagram
-
-
-
-
?
desmin + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
E-(EDANS)-PLFAERK-(Dabcyl) + H2O
?
show the reaction diagram
-
-
-
-
?
E-(Edans-)PLF-AERK-(Dabcyl) + H2O
?
show the reaction diagram
-
-
-
-
?
filamin A + H2O
?
show the reaction diagram
-
-
-
-
?
filamin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
fluorescin thiocarbamoyl-labeled casein + H2O
?
show the reaction diagram
-
-
-
-
?
fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
Frizzled-7 + H2O
?
show the reaction diagram
-
-, calpain-1 is a regulator of Frizzled-7 turnover at the plasma membrane
-
-
?
full-length glutamic acid decraboxylase67 + H2O
truncated glutamic acid decarboxylase67 + ?
show the reaction diagram
-
-, 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
?
show the reaction diagram
-
-
-
-
?
gamma-filamin + H2O
?
show the reaction diagram
-
phosphorylation of the filamin C-terminus domain by PKCalpha protects gamma-filamin against proteolysis by calpain 1 in COS cells
-
-
?
Hsp70.1 + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
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
-
-
?
I-kappaBalpha polymer + H2O
?
show the reaction diagram
-
-
-
-
?
insulin-like growth factor binding protein-2 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
-
-
?
integrin + H2O
?
show the reaction diagram
-
-
-
-
?
integrin beta3 + H2O
?
show the reaction diagram
-
-
-
-
?
K-(5(6)-carboxyfluorescein)-EVYGMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH + H2O
K-(5(6)-carboxyfluorescein)-EVY + GMMK(4-(4-dimethylaminophenylazo)benzoyl)-OH
show the reaction diagram
-
-
-
-
?
L-plastin + H2O
?
show the reaction diagram
-
L-plastin interaction with integrin is regulated through cleavage of beta-integrin by micro-calpain
-
-
?
LIS1 protein + H2O
?
show the reaction diagram
-
-
-
-
?
MAP2 + H2O
?
show the reaction diagram
-
-
-
-
?
MAP2 + H2O
?
show the reaction diagram
-
-
-
-
?
mature apoptosis-inducing factor (62 kDa) + H2O
cleaved apoptosis-inducing factor (57 kDa) + ?
show the reaction diagram
-
cleaved by the mitochondrial mu-calpain near its N-terminus
-
-
?
microtubule-associated protein 1
?
show the reaction diagram
-
-
-
-
?
microtubule-associated protein 2
?
show the reaction diagram
-
-
-
-
?
microtubule-associated protein 2 + H2O
?
show the reaction diagram
-
calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2
-
-
?
myelin-associated glycoprotein + H2O
?
show the reaction diagram
-
-, calpain overexpression due to *OH stress, IFN-gamma stimulation, or Ca2+ influx is involved in C6 cell death
-
-
?
myofibrillar protein + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-LLY-7-amido-4-fluromethylcoumarin + H2O
N-acetyl-LLY + 7-amino-4-fluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-4-methoxy-2-naphthylamide + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Leu-L-Arg-7-amido-4-trifluoromethylcoumarin + H2O
N-benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-L-leucyl-L-valyl-L-tyrosinyl-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-succinyl-LLVY-7-amido-4-methylcoumarin + H2O
N-succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Na+/Ca2+ exchanger isoform 3 + H2O
?
show the reaction diagram
-
-
-
-
?
neuronal calcium sensor-1 + H2O
?
show the reaction diagram
-
mu-calpain cleavage of neuronal calcium sensor-1 occurs within an N-terminal pseudoEF-hand domain (at Lys36), which is unable to bind Ca2+
-
-
?
neuronal nitric oxide synthase + H2O
?
show the reaction diagram
-
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
-
-
?
nNOS + H2O
?
show the reaction diagram
-
-
-
-
?
NR2 subunit of NMDA subtype of glutamate receptor + H2O
?
show the reaction diagram
-
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
-
-
?
p35 + H2O
p25 + ?
show the reaction diagram
-
-
-
-
?
plasma membrane Ca2+-ATPase isoform 1 + H2O
?
show the reaction diagram
-
readily and completely degraded by m-calpain
-
-
?
plasma membrane Ca2+-ATPase isoform 2 + H2O
?
show the reaction diagram
-
slow hydrolysis only to large fragments
-
-
?
plasma membrane Ca2+-ATPase isoform4 + H2O
?
show the reaction diagram
-
slow hydrolysis only to large fragments
-
-
?
podoplanin + H2O
?
show the reaction diagram
-
podoplanin stability is post-translationally regulated by calpain-1
-
-
?
pro-interleukin-33 + H2O
interleukin-33 + ?
show the reaction diagram
-
-
-
-
?
Rad21 + H2O
?
show the reaction diagram
-
calpain-1 cleaves Rad21 at Leu192
-
-
?
recombinant procaspase-3 + H2O
?
show the reaction diagram
-
-
-
-
?
recombinant procaspase-3 + H2O
?
show the reaction diagram
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
recombinant procaspase-9 + H2O
?
show the reaction diagram
-
-
-
-
?
recombinant procaspase-9 + H2O
?
show the reaction diagram
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
RecTat101 + H2O
?
show the reaction diagram
-
-
-
-
?
RhoA + H2O
?
show the reaction diagram
-
-, calpain cleaves RhoA and generates a form that inhibits integrin-induced stress fiber assembly and cell spreading
-
-
?
spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
show the reaction diagram
-
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-bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-bovine-serum-albumin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-casein + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-casein + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-insulin B + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-insulin B + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-L-Leu-L-Leu-L-Val-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Leu-L-Val + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
succinyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Met + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-L-Leu-L-Tyr-4-methoxy-2-naphthylamide + H2O
succinyl-L-Leu-L-Tyr + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
-
?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-L-Leu-L-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Tyr-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-LLVY-7-amido-4-methylcoumarin + H2O
succinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-protamine + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-protamine + H2O
?
show the reaction diagram
-
-
-
-
?
sucinyl-LLVY-7-amido-4-methylcoumarin + H2O
sucinyl-LLVY + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
talin + H2O
?
show the reaction diagram
-
-
-
-
?
talin + H2O
?
show the reaction diagram
-
-
-
-
?
tau protein + H2O
?
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-chloromethylcoumarin
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-L-Leu-L-Met-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-L-Met + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-L-leucyl-L-methionine-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-leucyl-L-methionine + 7-amino-4-chloromethylcoumarin
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Met + 7-amino-4-chloromethylcoumarin
show the reaction diagram
-
-
-
-
?
titin + H2O
?
show the reaction diagram
-
-
-
-
?
titin + H2O
?
show the reaction diagram
-
-
-
-
?
titin + H2O
?
show the reaction diagram
-
pH 7.5, absence or presence of 12 microM calcium
-
-
?
troponin + H2O
?
show the reaction diagram
-
-
-
-
?
troponin complex + H2O
?
show the reaction diagram
-
-
-
-
?
utrophin + H2O
?
show the reaction diagram
-
-
-
-
?
vimentin + H2O
?
show the reaction diagram
-
-
-
-
?
[2-Abz]-Ser-Thr-Phe-Ala-Gln-Pro-[3-nitrotyrosine]-NH2 + H2O
[2-Abz]-Ser-Thr-Phe + Ala-Gln-Pro-[3-nitrotyrosine]-NH2
show the reaction diagram
-
-
-
-
?
[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
?
show the reaction diagram
-
-
-
-
?
mitochondrial major Ca2+ extruding pathway Na+/Ca2+ exchanger + H2O
?
show the reaction diagram
-
cleaved by the mitochondrial mu-calpain
-
-
?
additional information
?
-
-
primary role of calpain 1 and calpain 3 in meat tenderization
-
-
-
additional information
?
-
P35750
enzyme is involved in myofibrillar protein degradation
-
-
-
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
?
-
-
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
?
-
-
age-dependent myelin degeneration and proteolysis of oligodendrocyte proteins is associated with the activation of calpain-1
-
-
-
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
?
-
-
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
?
-
-
mu-Calpain regulates receptor activator of NF-kappaB ligand (RANKL)-supported osteoclastogenesis via NF-kappaB activation in RAW 264.7 cells
-
-
-
additional information
?
-
P07384
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
?
-
-
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
?
-
-
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
?
-
-
role for mu-calpain isoform in the hypermeability of the diabetic endothelium
-
-
-
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
?
-
-
mitochondrial mu-calpain associates with ERp57, whereas, cytosolic mu-calpain does not associate with ERp57
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-actinin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
-
mu-calpain is neuroprotective in the earyl 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
-
-
?
alphaII-spectrin + H2O
?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
-
-
?
apoptosis-inducing factor + H2O
?
show the reaction diagram
-
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
truncated apoptosis-inducing factor + ?
show the reaction diagram
-
-
-
-
?
apoptosis-inducing factor + H2O
truncated apoptosis-inducing factor + ?
show the reaction diagram
-
mitochondrial micro-calpain is the protease responsible for processing apoptosis-inducing factor prior to its release
-
-
?
caspase-7 + H2O
?
show the reaction diagram
-
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
-
-
?
desmin + H2O
?
show the reaction diagram
-
-
-
-
?
filamin A + H2O
?
show the reaction diagram
-
-
-
-
?
filamin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
Frizzled-7 + H2O
?
show the reaction diagram
-
calpain-1 is a regulator of Frizzled-7 turnover at the plasma membrane
-
-
?
full-length glutamic acid decraboxylase67 + H2O
truncated glutamic acid decarboxylase67 + ?
show the reaction diagram
-
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
-
-
?
I-kappaBalpha polymer + H2O
?
show the reaction diagram
-
-
-
-
?
integrin + H2O
?
show the reaction diagram
-
-
-
-
?
MAP2 + H2O
?
show the reaction diagram
-
-
-
-
?
MAP2 + H2O
?
show the reaction diagram
-
-
-
-
?
mature apoptosis-inducing factor (62 kDa) + H2O
cleaved apoptosis-inducing factor (57 kDa) + ?
show the reaction diagram
-
cleaved by the mitochondrial mu-calpain near its N-terminus
-
-
?
microtubule-associated protein 2 + H2O
?
show the reaction diagram
-
calpain translates high-frequency Ca2+ transients into decomposition of its sensitive substrate microtubule-associated protein 2
-
-
?
myelin-associated glycoprotein + H2O
?
show the reaction diagram
-
calpain overexpression due to *OH stress, IFN-gamma stimulation, or Ca2+ influx is involved in C6 cell death
-
-
?
Na+/Ca2+ exchanger isoform 3 + H2O
?
show the reaction diagram
-
-
-
-
?
neuronal nitric oxide synthase + H2O
?
show the reaction diagram
-
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
-
-
?
p35 + H2O
p25 + ?
show the reaction diagram
-
-
-
-
?
Rad21 + H2O
?
show the reaction diagram
-
calpain-1 cleaves Rad21 at Leu192
-
-
?
recombinant procaspase-3 + H2O
?
show the reaction diagram
-
-
-
-
?
recombinant procaspase-3 + H2O
?
show the reaction diagram
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
recombinant procaspase-9 + H2O
?
show the reaction diagram
-
-
-
-
?
recombinant procaspase-9 + H2O
?
show the reaction diagram
-
calpain is a potential regulator of caspases and calpain promotes apoptosis-like events during platelet activation
-
-
?
RhoA + H2O
?
show the reaction diagram
-
calpain cleaves RhoA and generates a form that inhibits integrin-induced stress fiber assembly and cell spreading
-
-
?
spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
show the reaction diagram
-
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
-
-
?
talin + H2O
?
show the reaction diagram
-
-
-
-
?
talin + H2O
?
show the reaction diagram
-
-
-
-
?
tau protein + H2O
?
show the reaction diagram
-
-
-
-
?
titin + H2O
?
show the reaction diagram
-
-
-
-
?
troponin complex + H2O
?
show the reaction diagram
-
-
-
-
?
utrophin + H2O
?
show the reaction diagram
-
-
-
-
?
vimentin + H2O
?
show the reaction diagram
-
-
-
-
?
mitochondrial major Ca2+ extruding pathway Na+/Ca2+ exchanger + H2O
?
show the reaction diagram
-
cleaved by the mitochondrial mu-calpain
-
-
?
additional information
?
-
-
primary role of calpain 1 and calpain 3 in meat tenderization
-
-
-
additional information
?
-
P35750
enzyme is involved in myofibrillar protein degradation
-
-
-
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
?
-
-
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
?
-
-
age-dependent myelin degeneration and proteolysis of oligodendrocyte proteins is associated with the activation of calpain-1
-
-
-
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
?
-
-
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
?
-
-
mu-Calpain regulates receptor activator of NF-kappaB ligand (RANKL)-supported osteoclastogenesis via NF-kappaB activation in RAW 264.7 cells
-
-
-
additional information
?
-
P07384
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
?
-
-
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
?
-
-
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
?
-
-
role for mu-calpain isoform in the hypermeability of the diabetic endothelium
-
-
-
additional information
?
-
-
mu-calpain prefers Leu, Val or Ile at the P2 position and Lys, Tyr, Arg, or Met at the P1 position
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
activates
Ba2+
-
activates, Ka: 1.5 mM
Ca2+
-
half-maximal activity at 0.04 mM, maximal activity 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+
-
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+
-
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+
-
half-maximal activation at 0.04 mM
Ca2+
-
half-maximal activity at 0.02 mM, maximal activity at 0.1 mM
Ca2+
-
half-maximal activation at 0.03 mM, maximal activation at 0.1 mM
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+
-
half-maximal activation at 0.008 mM, maximal activation at 0.02 mM
Ca2+
-
half-maximal activation at 0.0028 mM, maximal activation at 0.01 mM
Ca2+
-
half-maximal activation at 0.01 mM
Ca2+
-
-
Ca2+
-
half-maximal activation at 0.002 mM, full activity at 0.01 mM
Ca2+
-
Ka-value : 0.05 mM
Ca2+
-
maximal activation at about 0.002 mM
Ca2+
-
sensitive to the frequency of fast Ca2+ oscillations in vitro
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+
-
mu-calpain is activated by neuronal stimulation and Ca2+-influx
Ca2+
-
0.0044 mM required for half-maximal activity
Ca2+
-
0.01 mM
Ca2+
-
calcium-dependent, increase of amount of bound calpain 1 by calcium binding to titin
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+
-
requires a micromolar concentration of Ca2+ for activity
Ca2+
-
the enzyme is Ca2+-dependent
Ca2+
-
calpain1 is a calcium ion-dependent cysteine protease
Ca2+
-
activates
Ca2+
-
activates at 1.0 mM
Ca2+
-
requires a micromolar concentration of calcium ions
Ca2+
-
micromolar (0.005-0.05 mM) Ca2+ concentrations are required for activation in vitro
Ca2+
-
the enzyme requires micromolar levels of Ca2+ for half-maximal activation
Ca2+
-
required
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+
-
required for activity
Ca2+
-
calcium-dependent cysteine protease
Ca2+
-
calpain I is a calcium-dependent protease
Ca2+
-
incubation with 5 mM Ca2+ results in the activation of micro-calpain
Ca2+
-
dependent on
Ca2+
-
dependent on
Ca2+
-
the enzyme requires micromolar calcium concentrations for activation
Ca2+
-
Ca2+ requirement for half-maximal activation (0.003-0.05 mM)
Ca2+
-
activity is absolutely dependent on calcium
Ca2+
-
dependent on, dysfunctional mitochondria increase cytosolic calcium, thereby inducing calpain activation
Ca2+
-
dependent on
Ca2+
-
calpain 1 is activated by micromolar calcium concentrations
Ca2+
-
activation of mu-calpain requires micromolar calcium (0.4 mM used in assays)
Ca2+
-
dependent on
Ca2+
-
dependent on
Ca2+
-
dependent on
Mn2+
-
synergistic acivation in combination with Ca2+
Mn2+
-
0.1 mM, less than 10% as active as Ca2+
Mn2+
-
activates
Mn2+
-
slight activation
Sr2+
-
synergistic acivation in combination with Ca2+
Sr2+
-
0.1 mM, less than 10% as active as Ca2+
Sr2+
-
activates
Sr2+
-
activates, Ka: 0.45 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
(-)-epicatechin 5-gallate
-
-
(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
(2S,5S)-5-benzyl-6-hydroxy-2-(2-methylpropyl)morpholin-3-one
-
SNJ-1757
(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
(4S)-3-[(4-methylphenyl)sulfonyl]-N-(1-oxo-3-phenylpropan-2-yl)-1,3-thiazolidine-4-carboxamide
-
-
(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-[(4-methylphenyl)sulfonyl]-N-(1-oxo-3-phenylpropan-2-yl)-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-fluorophenyl)amino]-8-phenylquinolin-4(1H)-one
-
-
3-acetyl-2-[(4-chlorophenyl)amino]-5,8-difluoroquinolin-4(1H)-one
-
-
3-acetyl-2-[(4-tert-butylphenyl)amino]-5,8-difluoroquinolin-4(1H)-one
-
-
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
-
-
3-acetyl-2-[[3,5-bis(trifluoromethyl)phenyl]amino]-5,8-difluoroquinolin-4(1H)-one
-
-
3-acetyl-5,8-dibromo-2-[(4-bromophenyl)amino]quinolin-4(1H)-one
-
-
3-acetyl-5,8-dichloro-2-[(2,4-dichlorophenyl)amino]quinolin-4(1H)-one
-
-
3-acetyl-6,8-difluoro-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
-
-
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-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-bromo-5-chloro-2-[(4-chlorophenyl)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-[(3-methylphenyl)amino]-5-nitroquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(4-chloro-2-fluorophenyl)amino]-5-methylquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-2-[(4-chlorophenyl)amino]-6-nitroquinolin-4(1H)-one
-
-
3-acetyl-8-chloro-5-fluoro-2-(phenylamino)quinolin-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
-
-
acetyl-calpastatin peptide
-
50 microM
-
acetyl-DPMSSTYIEE-betaAla-GKREVTIPPKYRELLA-NH2
-
-
-
acetyl-DPMSSTYIEELGK-NH2
-
-
acetyl-DPMSSTYIEELGKREVT-betaAla-PPKYRELLA-NH2
-
-
-
acetyl-DPMSSTYIEELGKREVTIPPKYR-NH2
-
-
acetyl-DPMSSTYIEELGKREVTIPPKYREL-NH2
-
-
acetyl-DPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
CP1B peptide
-
acetyl-Leu-Leu-Met-CHO
-
-
acetyl-Leu-Leu-Nle-CHO
-
-
acetyl-Leu-Leu-Nle-CHO
-
a calpain inhibitor
acetyl-Leu-Leu-Nle-CHO
-
-
acetyl-REVTIPPKYRELLA-NH2
-
-
acetyl-RRMKWKKDPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
-
-
acetyl-RYKPPITVERKGLEEIYTSS-NH2
-
-
acetyl-SSTTYIEELGKREVTIPPKYR-NH2
-
-
-
acetyl-SSTYIEELGK-NH-(CH2O)2-CH2C(O)-TIPPKYR-NH2
-
-
acetyl-SSTYIEELGKREVTIPPK-NH2
-
-
acetyl-SSTYIEELGKREVTIPPKYR-NH2
-
-
acetyl-SSTYIEELGKREVTIPPKYRELLA-NH2
-
-
acetyl-TYIEELGKREVTIPPKYR-NH2
-
-
acetyl-TYIEELGKREVTIPPKYRELLA-NH2
-
-
AK-275
-
reversible inhibitor
-
AK-295
-
reversible inhibitor
AK-295-D1
-
reversible inhibitor
-
AK-295-D2
-
reversible inhibitor
-
Al3+
-
inactivates enzyme from smooth muscle at millimolar concentrations of Ca2+, calpain 1 and 2
ALLM
-
reversible inhibitor
ALLN
-
reversible inhibitor
antipain
-
0.01 mM, 80-90% inhibition
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
-
-
Calmidazolium
-
-
calpain inhibitor 1
-
synthetic calpain inhibitor
calpain inhibitor III
-
-
calpain inhibitor III
-
-
calpain inhibitor peptide III
-
-
calpain inhibitor VI
-
-
calpain inhibitor-1
-
-
calpain inhibitor-1
-
-
calpain inhibitor-III
-
-
calpain inhibitor-III
-
-
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
-
Calpastatin
-
mitochondrial mu-calpain is tightly regulated by its endogenous inhibitor calpastatin
-
Calpastatin
-
highly specific inhibitor of calpain-1 and calpain-2
-
Calpastatin
-
broad-spectrum calpain inhibitor
-
Calpastatin
-
-
-
Calpastatin
-
highly specific calpain inhibitor
-
calpastatin 1
-
capain 1 is under constant inhibiting effect of active calpastatin 1
-
calpastatin peptides
-
-
-
Calpeptin
-
reversible inhibitor
Calpeptin
-
Z-Leu-Nle-CHO
Calpeptin
-
complete inhibition at 0.5 mM
carbobenzoxy-valinyl-phenylalaninal
-
-
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
-
E-64
-
0.05 mg/ml, complete inhibition
E-64
-
irreversible inhibitor
E-64c
-
0.01 mM, 80-90% inhibition
E-64c
-
irreversible inhibitor
E-64d
-
irreversible inhibitor
EDTA
-
0.25 mM, complete
Ep-460
-
irreversible inhibitor
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
inhibitor protein Ci1
-
non-specific inhibitor
-
iodoacetic acid
-
0.25 mM, complete
ionomycin
-
-
lactacystin
-
1 microM
Leupeptin
-
0.05 mg/ml, complete inhibition
Leupeptin
-
-
Leupeptin
-
0.01 mM, 80-90% inhibition
Leupeptin
-
-
Leupeptin
-
a naturally occurring calpain inhibitor
Leupeptin
-
reversible inhibitor
MDL-28170
-
reversible inhibitor
MDL-28170
-
Cbz-Val-Phel-alanial
MDL-28170
-
-
MDL-28170
-
-
MDL-28170
-
-
MDL-28710
-
complete inhibition at 100 nM
MDL28170
-
potent inhibitor of the active site of calpain1
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
-
-
MG115
-
inhibitory effect in micromolar concentrations, 1 mircoM
MG132
-
inhibitory effect in micromolar concentrations, 1 microM
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)-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-acetyl-L-Leu-L-Leu-L-Met
-
-
N-acetyl-L-leucyl-L-leucyl-L-norleucinal
-
broad-spectrum calpain inhibitor
N-acetyl-Leu-Leu-Nle-CHO
-
complete inhibition at 0.5 mM
-
N-acetyl-Leu-Leu-Norleu-al
-
-
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-2-oxoethyl]-N2-[(benzyloxy)carbonyl]-L-leucinamide
-
-
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-[[(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
NaCl
-
mu-calpain is more active at 165 mM NaCl than at 295 mM NaCl
PCP1B peptide
-
-
-
PD-150606
-
-
PD-151746
-
-
PD150606
-
specific inhibitor of calpain I
PD150606
-
-
penetratin
-
-
penicillide
-
-
pepstatin A
-
1 mM, 60-80% inhibition
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
SJA-6017
-
reversible inhibitor
SNJ-1715
-
reversible inhibitor
SNJ-1945
-
reversible inhibitor
SNJ1715
-
-
TLCK
-
0.1 mM, 60-80% inhibition
Z-Val-Phe-CHO
-
i.e. MDL-28710, 1.0 microM
ZLLY-CH2F
-
irreversible inhibitor
additional information
-
specific capn1 shRNA reduces expression of the targeted isoform
-
additional information
-
FANCA and FANCG proteins bind directly to mu-calpain, this binding may lead to inhibition of mu-calpain activity in normal cells
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
required for maximal activity
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
NS5A protein
-
the nonstructural hepatitis C virus protein NS5Ais sufficient to activate a calpain 1
-
endotoxin
-
treatment with 12 mg/kg endotoxin increases diaphragm calpain activity and active calpain I protein
-
additional information
-
no influence on expression of calpain-1 by mechanical stimulation
-
additional information
-
HRSP12 (UK114) stimulates the hydrolysis activity of Calpain1
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
-
0.053
-
casein
-
pH and temperature not specified in the publication
0.0131
-
fluorescin thiocarbamoyl-labeled casein
-
pH and temperature not specified in the publication
-
5e-05
-
fodrin
-
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
0.002
-
succinyl-bovine serum albumin
-
pH and temperature not specified in the publication
-
2
-
succinyl-bovine-serum albumin
-
pH 7.5, 25C
-
0.0081
-
succinyl-casein
-
pH 7.5, 25C
-
0.0081
-
succinyl-casein
-
pH and temperature not specified in the publication
-
0.284
-
succinyl-insulin B
-
pH and temperature not specified in the publication
-
283.5
-
succinyl-insulin B
-
pH 7.5, 25C
-
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
0.063
-
succinyl-protamine
-
pH and temperature not specified in the publication
-
63
-
succinyl-protamine
-
pH 7.5, 25C
-
5.9
-
tert-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
-
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8.1e-05
-
1-[(4-methylphenyl)sulfonyl]-N-(1-oxo-3-phenylpropan-2-yl)-D-prolinamide
-
pH and temperature not specified in the publication
8.5e-06
-
3-([N-[(benzyloxy)carbonyl]-L-leucyl]amino)-2-oxo-4-phenylbutanoic acid
-
pH and temperature not specified in the publication
5e-05
-
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
-
0.0069
-
acetyl-DPMSSTYIEELGK-NH2
-
pH 7.5, 12C
0.0024
-
acetyl-DPMSSTYIEELGKREVT-betaAla-PPKYRELLA-NH2
-
pH and temperature not specified in the publication
-
8e-07
-
acetyl-DPMSSTYIEELGKREVTIPPKYR-NH2
-
pH 7.5, 12C
5e-07
-
acetyl-DPMSSTYIEELGKREVTIPPKYREL-NH2
-
pH 7.5, 12C
2e-07
-
acetyl-DPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
-
0.035
-
acetyl-REVTIPPKYRELLA-NH2
-
pH 7.5, 12C
1.9e-07
-
acetyl-RRMKWKKDPMSSTYIEELGKREVTIPPKYRELLA-NH2
-
pH and temperature not specified in the publication
-
0.726
-
acetyl-RYKPPITVERKGLEEIYTSS-NH2
-
pH 7.5, 12C
2.6e-05
-
acetyl-SSTTYIEELGKREVTIPPKYR-NH2
-
pH and temperature not specified in the publication
-
0.0117
-
acetyl-SSTYIEELGK-NH-(CH2O)2-CH2C(O)-TIPPKYR-NH2
-
pH 7.5, 12C
0.017
-
acetyl-SSTYIEELGKREVTIPPK-NH2
-
pH 7.5, 12C
2.6e-05
-
acetyl-SSTYIEELGKREVTIPPKYR-NH2
-
pH 7.5, 12C
6e-07
-
acetyl-SSTYIEELGKREVTIPPKYRELLA-NH2
-
pH 7.5, 12C
9.3e-05
-
acetyl-TYIEELGKREVTIPPKYR-NH2
-
pH 7.5, 12C
9.3e-05
-
acetyl-TYIEELGKREVTIPPKYR-NH2
-
pH and temperature not specified in the publication
2.2e-06
-
acetyl-TYIEELGKREVTIPPKYRELLA-NH2
-
pH 7.5, 12C
2.6e-05
-
CP1B peptide
-
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
9e-06
-
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
2.7e-05
-
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
4.7e-06
-
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
2e-05
-
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
0.0002
-
N2-[(benzyloxy)carbonyl]-N-[4-(ethylamino)-3,4-dioxo-1-phenylbutan-2-yl]-L-leucinamide
-
pH and temperature not specified in the publication
5e-07
-
PCP1B peptide
-
pH and temperature not specified in the publication
-
1.8e-07
-
penetratin
-
pH and temperature not specified in the publication
0.0059
-
ritonavir
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00088
-
(2S)-2-[[(4-fluorophenyl)sulfonyl]amino]-N-[(3S)-2-hydroxytetrahydrofuran-3-yl]-3-methylbutanamide
-
pH and temperature not specified in the publication
0.0007
-
(2S,5S)-5-benzyl-6-hydroxy-2-(2-methylpropyl)morpholin-3-one
-
pH and temperature not specified in the publication
3.8e-05
-
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(10H-phenothiazin-2-yloxy)acetyl]-L-threonyl-L-leucinate
-
pH and temperature not specified in the publication
8.9e-05
-
(3S)-2-hydroxytetrahydrofuran-3-yl N-[(2S)-2-[[(10H-phenothiazin-2-yloxy)acetyl]amino]butanoyl]-L-leucinate
-
pH and temperature not specified in the publication
0.001
-
(3S)-3-[[N-(10H-phenothiazin-2-ylcarbonyl)-L-norvalyl]amino]tetrahydrofuran-2-yl acetate
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
-
0.0005
-
1-(2-chloro-4-hydroxyphenyl)-4-oxo-7-(pyridin-4-yl)-1,4-dihydroquinoline-3-carboxamide
-
pH and temperature not specified in the publication
6e-06
-
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
-
pH and temperature not specified in the publication
5.6e-05
-
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
5.6e-05
-
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
0.00034
-
3-([4-[2-(methoxymethoxy)phenyl]-4-oxobutanoyl]amino)-2-oxo-4-phenylbutanamide
-
pH and temperature not specified in the publication
0.0192
-
3-acetyl-2-[(2,4-dichlorophenyl)amino]-8-(trifluoromethyl)quinolin-4(1H)-one
-
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 25C
0.03
-
3-acetyl-2-[(3-fluorophenyl)amino]-8-phenylquinolin-4(1H)-one
-
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 25C
0.03
-
3-acetyl-2-[(4-chlorophenyl)amino]-5,8-difluoroquinolin-4(1H)-one
-
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 25C
0.03
-
3-acetyl-2-[(4-tert-butylphenyl)amino]-5,8-difluoroquinolin-4(1H)-one
-
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 25C
0.00369
-
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
-
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 25C
0.00743
-
3-acetyl-2-[(4-tert-butylphenyl)amino]-8-chloro-6-nitroquinolin-4(1H)-one
-
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 25C, pH 7.5
0.03
-
3-acetyl-2-[[3,5-bis(trifluoromethyl)phenyl]amino]-5,8-difluoroquinolin-4(1H)-one
-
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 25C
0.00169
-
3-acetyl-5,8-dibromo-2-[(4-bromophenyl)amino]quinolin-4(1H)-one
-
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 25C, pH 7.5
0.00359
-
3-acetyl-5,8-dibromo-2-[(4-bromophenyl)amino]quinolin-4(1H)-one
-
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 25C
0.00317
-
3-acetyl-5,8-dichloro-2-[(2,4-dichlorophenyl)amino]quinolin-4(1H)-one
-
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 25C, pH 7.5
0.00399
-
3-acetyl-5,8-dichloro-2-[(2,4-dichlorophenyl)amino]quinolin-4(1H)-one
-
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 25C
0.03
-
3-acetyl-6,8-difluoro-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
-
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 25C
0.00316
-
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-4(1H)-one
-
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 25C, pH 7.5
0.00464
-
3-acetyl-6-chloro-2-[(2,4-dichlorophenyl)amino]-8-nitroquinolin-4(1H)-one
-
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 25C
0.00239
-
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
-
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 25C, pH 7.5
0.00373
-
3-acetyl-6-chloro-2-[(2-chloro-4-methylphenyl)amino]-8-nitroquinolin-4(1H)-one
-
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 25C
0.03
-
3-acetyl-6-chloro-8-(trifluoromethyl)-2-[[4-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
-
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 25C
0.03
-
3-acetyl-7,8-dichloro-2-[[3-(trifluoromethyl)phenyl]amino]quinolin-4(1H)-one
-
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 25C
0.00353
-
3-acetyl-8-bromo-5-chloro-2-[(4-chlorophenyl)amino]quinolin-4(1H)-one
-
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 25C
0.00994
-
3-acetyl-8-bromo-5-chloro-2-[(4-chlorophenyl)amino]quinolin-4(1H)-one
-
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 25C, pH 7.5
0.000277
-
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
-
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 25C
0.00028
-
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
-
pH and temperature not specified in the publication
0.00306
-
3-acetyl-8-chloro-2-[(2,4-dibromophenyl)amino]-5-methylquinolin-4(1H)-one
-
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 25C, pH 7.5
0.03
-
3-acetyl-8-chloro-2-[(2-fluoro-5-methylphenyl)amino]-5-(trifluoromethyl)quinolin-4(1H)-one
-
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 25C
0.03
-
3-acetyl-8-chloro-2-[(3-methylphenyl)amino]-5-nitroquinolin-4(1H)-one
-
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 25C
0.03
-
3-acetyl-8-chloro-2-[(4-chloro-2-fluorophenyl)amino]-5-methylquinolin-4(1H)-one
-
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 25C
0.00456
-
3-acetyl-8-chloro-2-[(4-chlorophenyl)amino]-6-nitroquinolin-4(1H)-one
-
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 25C
0.00808
-
3-acetyl-8-chloro-2-[(4-chlorophenyl)amino]-6-nitroquinolin-4(1H)-one
-
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 25C, pH 7.5
0.03
-
3-acetyl-8-chloro-5-fluoro-2-(phenylamino)quinolin-4(1H)-one
-
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 25C
0.03
-
3-acetyl-8-chloro-5-methyl-2-[(2,3,4-trifluorophenyl)amino]quinolin-4(1H)-one
-
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 25C
0.03
-
3-acetyl-8-chloro-5-methyl-2-[(2,4,5-trifluorophenyl)amino]quinolin-4(1H)-one
-
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 25C
2.9e-05
-
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
5e-05
-
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
4.7e-05
-
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
5e-05
-
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
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
-
-
0.00033
-
5-azanylidyne-N-[[(2S,3S)-3-(ethoxycarbonyl)oxiran-2-yl]carbonyl]-L-norvalyl-L-arginyl-L-tryptophanamide
-
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
-
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
-
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
-
pH and temperature not specified in the publication
0.00019
-
acetyl-Leu-Leu-Nle-CHO
-
pH and temperature not specified in the publication
85
-
benzyl (2Z)-[(3S)-3-sec-butyl-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetate
-
-
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
-
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
-
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
-
pH and temperature not specified in the publication
8e-06
-
calpain inhibitor III
-
pH and temperature not specified in the publication
7.5e-06
-
calpain inhibitor VI
-
pH and temperature not specified in the publication
5.2e-05
-
Calpeptin
-
pH and temperature not specified in the publication
6.4e-05
-
dimethyl (2S,2'S)-2,2'-[biphenyl-2,2'-diylbis(carbonylimino)]bis(3-phenylpropanoate)
-
pH and temperature not specified in the publication
0.0015
-
E-64
-
-
0.000199
-
MDL28170
-
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 25C, pH 7.5
0.0002
-
MDL28170
-
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 25C, pH 7.5
8.9e-05
-
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
2.5e-05
-
methyl (2Z)-[(3S)-3-sec-butyl-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetate
-
-
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
-
IC50: 1000 nM
2.5e-05
-
methyl (S,S,Z)-(3-sec-butyl-1-oxo-2,3-dihydro-1H-isoquinolin-4-ylidene)acetate
-
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
-
-
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
-
-
6.6e-05
-
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-leucyl-L-phenylalaninate
-
-
0.000626
-
methyl N-[(2Z)-2-[(3S)-3-(1-methylpropyl)-1-oxo-2,3-dihydroisoquinolin-4(1H)-ylidene]acetyl]-L-valyl-L-phenylalaninate
-
-
8.7e-08
-
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
-
pH and temperature not specified in the publication
2e-05
-
N'-((1S,2R)-1-benzyl-3-[(3,5-dimethoxybenzyl)amino]-2-hydroxypropyl)-N,N-dipropylbenzene-1,3-dicarboxamide
-
IC50: 20 nM
6.3e-05
-
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
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
-
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
-
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
-
IC50: 286 nM
0.00071
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-1,4-dihydroquinoline-2-carboxamide
-
pH and temperature not specified in the publication
4e-05
-
N-(4-amino-3,4-dioxo-1-phenylbutan-2-yl)-3-methyl-4-oxo-4H-chromene-2-carboxamide
-
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
-
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
-
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
-
IC50: 200 nM
0.00024
-
N-[(1S)-1-benzyl-2-oxoethyl]-N2-[(benzyloxy)carbonyl]-L-leucinamide
-
-
8.1e-05
-
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
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
-
IC50: 340 nM
2.8e-05
-
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
-
pH and temperature not specified in the publication
2.3e-05
-
N-[(2S)-1-[[(3S)-2-hydroxytetrahydrofuran-3-yl]amino]-1-oxopentan-2-yl]-10H-phenothiazine-2-carboxamide
-
pH and temperature not specified in the publication
3.5e-05
-
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
-
pH and temperature not specified in the publication
5e-05
-
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
-
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
-
pH and temperature not specified in the publication
5e-05
-
N-[[(1R)-1-phenyl-2-(4-propoxyphenyl)ethoxy]carbonyl]glycyl-N-[(2S)-1-oxopentan-2-yl]-L-leucinamide
-
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
-
pH and temperature not specified in the publication
7.6e-05
-
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
4e-05
-
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
3.5e-05
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
mu-calpain
7.3
-
-
monomeric calpain I
7.5
-
-
-
7.5
-
-
dimeric calpain I
7.5
-
-
enzyme in mitochondrial lysate
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8
-
pH 6.5: about 35% of maximal activity, pH 8.0: about 50% of maximal activity
6.5
-
-
m-calpain
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
-
37
-
-
assay at 37C, 20 min, with or without magnetic bead stimulation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
-
activation of mu-calpain in platelets from patients with type 2 diabetes mellitus
Manually annotated by BRENDA team
-
white matter from patients with MS and Parkinsons and Alzheimers diseases and white matter from normal control
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
from patients with recurrent miscarriage and healthy women with informed consent
Manually annotated by BRENDA team
-
from Shumiya cataract animals
Manually annotated by BRENDA team
-
calpain 1 is most abundant in cells near the lens surface
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
postmortem muscle
Manually annotated by BRENDA team
-
loss of activity during postmortem aging
Manually annotated by BRENDA team
-
loss of activity during postmortem aging
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
rheumatic synovial cell line. mu-calpain, regulates MMP-3 release by rheumatic synovial cells, in addition to exerting its own degradative action on cartilage
Manually annotated by BRENDA team
-
first molar of foetal ICR mice from embryonic day 14 to postnatal day 7
Manually annotated by BRENDA team
-
musculus longissimus, postmortem muscle
Manually annotated by BRENDA team
-
musculus longissimus thoracis et lumborum, loss of activity during postmortem aging
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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 25C
Manually annotated by BRENDA team
-
NO-induced motility in osteoclasts requires regulated Ca2+ release, which activates mu-calpain. This occurs via the inositol (1,4,5)-trisphosphate receptor 1
Manually annotated by BRENDA team
-
originated from kidney
Manually annotated by BRENDA team
-
psoas major, loss of activity during postmortem aging
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Plasmodium falciparum FCR-3
-
-
-
Manually annotated by BRENDA team
-
loss of activity during postmortem aging
Manually annotated by BRENDA team
-
neuroblastoma
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
localisation in the Z-band and under the plasma membrane
Manually annotated by BRENDA team
-
excentric exercise produces little autolytic activation of mu-calapin
Manually annotated by BRENDA team
-
musculus sternomandibularis
Manually annotated by BRENDA team
-
in skeletal muscle, mu-calpain is a freely diffusible protein
Manually annotated by BRENDA team
Plasmodium falciparum FCR-3
-
-
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
additional information
-
not detected in testis
Manually annotated by BRENDA team
additional information
Plasmodium falciparum FCR-3
-
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
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
calpain-1 is relocated and translocated from cytoplasm to plasma membrane during capacitation
Manually annotated by BRENDA team
Plasmodium falciparum FCR-3
-
-
-
Manually annotated by BRENDA team
-
diffusely located in cytosol
Manually annotated by BRENDA team
-
neuronal cytosol
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
association between l-calpain and calpastatin in the mitochondria
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
mu-calpain, including both the large and small subunits is present in the mitochondrial intermembrane space
Manually annotated by BRENDA team
-
a pool of micro-calpain is localized to the mitochondrial intermembrane space
Manually annotated by BRENDA team
-
present mostly in the intermembrane space
Manually annotated by BRENDA team
-
calpain-1 normally localizes to the interphase nuclei and chromatin
Manually annotated by BRENDA team
-
calpain-1 is relocated and translocated from cytoplasm to plasma membrane during capacitation
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
46000
-
-
recombinant enzyme, gel filtration
80000
-
-
gel filtration
80000
-
-
SDS-PAGE
80000
-
-
full-length isoform
80000
-
-
SDS-PAGE
80000
-
-
subunit, SDS-PAGE
80000
-
-
about 80000 Da, SDS-PAGE
88000
-
-
gel filtration
110000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 80000, SDS-PAGE
dimer
-
1 * 74000 + 1 * 32000, SDS-PAGE
dimer
-
1 * 80000 + 1 * 28000, SDS-PAGE
dimer
-
1 * 83000 + 1 * 29000, an isolated 70000 Da calpain I, or monomeric artifact is also detected, SDS-PAGE
dimer
-
1 * 83000 + 1 * 29000, SDS-PAGE
dimer
-
1 * 74000 + 1 * 32000, both subunits are catalytically active, SDS-PAGE
dimer
-
1 * 76000 + 1 * 28000, SDS-PAGE
dimer
-
-
dimer
-
1 * 80000 + 1 * 25000, SDS-PAGE
dimer
-
1 * 80000 + x * ?, SDS-PAGE
heterodimer
-
-
heterodimer
-
-
heterodimer
-
1 * 80000 + 1 * 30000, SDS-PAGE
heterodimer
-
1 * 80000 + 1 * 28000
heterodimer
-
1 * 80000 + 1 * 28000, 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
-
Ca2+ causes autoproteolytic conversion of the native 80000 Da subunit into the active 75000 Da subunit
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
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
-
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
-
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
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
the 70000 Da monomeric calpain I is less pH stable than the parent heterodimeric calpain I
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
58
-
-
10 min, stable
58
-
-
10 min, more than 30% of the original activity is left
60
-
-
10 min, 15% loss of activity
additional information
-
-
the 70000 Da monomeric calpain I is much less heat stable than the parent heterodimeric calpain I
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
30% inactivation by trypsin after 15 min at 30C, pH 7.5
-
5% autolysis after 10 min, at 0C, pH 7.5, 10 mM Ca2+
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
affinity chromatography, calmodulin-like domain of the catalytic subunit expressed in E. coli
-
Ni2+-NTA-agarose column chromatography
-
purification of a 21000 Da calpain small subunit fragment
-
E-F hand structure domains
-
Ni-NTA column chromatography
-
large scale
-
mu-calpain
-
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression of mutant enzyme C115S in insect cell using a baculovirus system
-
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
-
large subunit
-
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
-
expressed in Escherichia coli BL21 cells
-
small subunit and large subunit
P97571
a 289 bp fragment for mu-calpain is cloned into the EcoRV site of pBluescript II KS+ vector
P35750
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
-
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))
-
in comparison to the sham operation group, the activity of calpain I is significantly increased (2.3fold) in the control atrial fibrillation group
-
WNT5A knockdown decreases calpain 1 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
-
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
-
fatiguing jumping exercise does not change mRNA expression of calpain 1
-
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
-
calpain-I is activated in human carotid plaques
-
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
-
after cisplatin treatment, calpain activation is an early event
-
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
-
Wnt5A activates calpain-1, leading to the cleavage of filamin A
-
cold storage (at 4C) 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
-
compared to control cybrids, Parkonsins disease cybrids reveal a significant increase in calpain activity
-
in mice with myocardial infarction, calpeptin treatment causes a significant decrease in micro-calpain level
-
compared with 5-month-old mice, there is no change in calpain 1 in 16-month-old mice
-
mu-calpain expression levels are unchanged by laminar shear flow or disturbed shear flow stimulus
-
in healthy mice, calpeptin treatment causes a significant increase in micro-calpain
-
treatment with 12 mg/kg endotoxin increases active calpain I protein
-
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
-
listeriolysin O-dependent bacterial entry into the cytoplasm is required for calpain activation and interleukin-1 alpha secretion in macrophages infected with Listeria monocytogenes
-
in cultured pulmonary microvascular endothelial cells, incubation with septic plasma stimulates calpain activation. Reactive oxygen species produced from NADPH oxidase stimulates calpain-1 activation
-
calpain activity in liver of heterozygous cystathionine beta synthase-deficient mice shows a 30% increase compared to wild type mice
-
mitochondrial mu-calpain activity is increased by 160% during ischemia-reperfusion compared to time control
-
inner ear cell death due to apoptosis occurs in a time-dependent manner with concomitant up-regulation of calpain-I expression
-
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)
-
MK801 added shortly after glutamate prevents calpain 1 activation
-
mu-calpain activity decreases by about 37% immediately and 2 h after acute-exhaustive exercise
-
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
-
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
-
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
-
delayed calcium deregulation is not sufficient to activate calpain 1
-
mu-calpain is activated in neurons after ischemia
-
high glucose (33 mM) induces calpain-1 activation in cardiomyocytes. Gp91phox-NADPH oxidase contributes to calpain-1 activation in high glucose-induced cardiomyocytes
-
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
-
ionomycin and thapsigragin, which elevate [Ca2+], activate calpains in cells exposed to normoxia
-
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
P35750
Protein Never in Mitosis Gene A Interacting-1 reduces calpain activity and slows the degradation of COX-2 in MAEC cells
-
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
-
low nutritional level diet treatment increases mRNA level of micro-calpain in skeletal muscle
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C115A
-
non-autolysing active-site mutant
C115S
-
mutant without proteolytic activity of autolysis and caseinolysis
additional information
C6ERB9, C6ERC0, C6ERC1
the mu-calpain single nucleotide polymorphisms C80T, C302G, G310A, C445T, and A524C are associated with tenderness in beef cattle; the mu-calpain single nucleotide polymorphisms C80T, C302G, G310A, C445T, and A524C are associated with tenderness in beef cattle; 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
H272A
-
catalytically inactive
additional information
-
-
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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
presence of inhibitors during renaturation is necessary to prevent autolysis
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
-
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
-
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
-
calpain and calpain inhibition is a therapeutic tool in Parkinsons disease
medicine
-
calpain1 is a therapeutic target in HER2-positive breast cancer
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
-
the inhibition of calpain is a potential therapeutic intervention for lissencephaly
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-1 activation is important in the development of diabetic cardiomyopathy and thus represents a potential therapeutic target for diabetic heart diseases
medicine
-
mu-calpain can serve as an predictor of muscle injury