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alpha-2 spectrin + H2O
?
-
-
-
-
?
alpha-actin + H2O
?
-
slow degradation
-
-
?
alpha-adaptin + H2O
?
-
-
-
-
?
alpha-fodrin + H2O
?
-
-
-
-
?
alpha-neoendorphin + H2O
?
-
cleavage of the 6Arg-7Lys bond
-
-
?
alpha-spectrin + H2O
145000 Da fragment + ?
-
-
-
-
?
alpha-spectrin + H2O
?
-
-
-
-
?
alpha-tubulin + H2O
?
-
complete digestion of alpha-tubulin with little effect on beta-tubulin
-
-
?
aminopeptidase B + H2O
?
-
-
-
-
?
androgen receptor + H2O
?
-
-
-
-
?
androgen receptor + H2O
low molecular weight androgen receptor + ?
-
-
-
-
?
angiotensin + H2O
?
-
clevage of the 4tyr-5Ile bond
-
-
?
benzoyl-Arg p-nitroanilide + H2O
?
-
-
-
-
?
beta-lipotropin(61-91) + H2O
?
-
cleavage of the bonds: Thr76-Leu77, Lys84-Asn85 and Lys88-Lys89
-
-
?
beta-neoendorphin + H2O
?
-
cleavage of the 6Arg-7Lys bond
-
-
?
beta-subunit of coatomer complex beta-COP + H2O
?
-
-
-
-
?
beta-transducin repeat containing protein + H2O
?
-
-
-
-
?
beta2-adaptin + H2O
?
-
-
-
-
?
Boc-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
Boc-Leu-Met + 7-amino-4-chloromethylcoumarin
-
10 microM, 20 min, 37 °C, with or without magnetic bead stimulation
-
-
?
Boc-Leu-Met-7-amino-4-chloromethylcoumarin
?
-
-
-
-
?
Boc-Val-Leu-Lys-methylcoumarin + H2O
?
-
-
-
-
?
calmodulin-dependent protein kinase II deltaB + H2O
?
caspase-3 + H2O
?
-
-
-
-
?
collapsin response mediator protein 1 + H2O
?
-
-
-
-
?
collapsin response mediator protein 2 + H2O
?
-
-
-
-
?
collapsin response mediator protein 3 + H2O
?
-
-
-
-
?
collapsin response mediator protein 4 + H2O
?
-
-
-
-
?
collapsin response mediator protein-1 + H2O
?
-
collapsin response mediator protein-1 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-2 + H2O
?
-
collapsin response mediator protein-2 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-4 + H2O
?
-
collapsin response mediator protein-4 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-5 + H2O
?
-
-
-
-
?
cortactin + H2O
?
-
-
-
-
?
cyclin dependent kinase-5 + H2O
p25-CDK5
-
-
-
-
?
dihydropteridine reductase + H2O
?
-
the dihydropteridine reductase 29000 Da subunit is cleaved just before the 35th Ser and the 48th Val residue from the N-terminus, generating two new fragments of 21000 Da and 19000 Da which are more active than the native enzyme
-
-
?
dynorphin (1-13) + H2O
?
-
cleavage of the 6Arg-7Arg bond
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
filamin A + H2O
?
-
-
-
-
?
focal adhesion kinase + H2O
?
-
the preferred calpain cleavage site is between the two C-terminal proline-rich regions after Ser-745
-
-
?
frequenin homolog + H2O
?
-
-
-
-
?
FRET-based substrate PLFAER + H2O
?
10 microM, pH 7.4, 1 mM of CaCl2 added to initiate the reaction
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
heterogeneous nuclear ribonucleoprotein F + H2O
?
-
-
-
-
?
heterogeneous nuclear ribonucleoprotein K + H2O
?
-
-
-
-
?
internexin + H2O
?
-
-
-
-
?
IP3R1 + H2O
?
-
in presence of Ca2þ, m-calpain cleaves IP3R1 in the endoplasmic lumen
-
-
?
laminin receptor 1 + H2O
?
-
-
-
-
?
Leu-enkephalin + H2O
?
-
cleaved only slightly at the 1Tyr-2Gly bond
-
-
?
mammalian actin-binding protein-1 + H2O
?
-
the preferred cleavage site occurs between the actin-binding domain and the proline-rich region, generating a C-terminal mAbp1 fragment
-
-
?
Met-enkephalin + H2O
?
-
cleaved only slightly at the 1Tyr-2Gly bond
-
-
?
microtubule-associated protein 1
?
-
-
-
-
?
microtubule-associated protein 1B + H2O
?
-
-
-
-
?
microtubule-associated protein 2
?
-
-
-
-
?
myosin II heavy chain + H2O
?
-
rapid proteolysis
-
-
?
N-acetyl-LLY-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-LLY + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
Na+/Ca2+ exchanger + H2O
82000 Da fragment + ?
-
-
-
-
?
Na+/Ca2+ exchanger-1 + H2O
82 kDa fragment + ?
-
calcium-dependent proteolytic cleavage of Na+/Ca2+ exchanger-1 occurs in the caveolae vesicles
-
-
?
neurofilament + H2O
?
-
-
-
-
?
neurotensin + H2O
?
-
cleavage of the 3Tyr-4Glu bond and the 5Asn-6Lys bond
-
-
?
nucleolin + H2O
?
-
-
-
-
?
p35 + H2O
25000 Da fragment of p35 + ?
-
calpain-specific substrate
-
-
?
proteolysis-resistant fragment 130 + H2O
proteolysis-resistant fragment 45 + ?
-
-
-
-
?
proteolysis-resistant fragment 72 + H2O
proteolysis-resistant fragment 45 + ?
-
-
-
-
?
RRRRRRRR-(EDANS)-GQQEVYGMMPRDG-(DABCYL) + H2O
?
-
-
-
-
?
selenoprotein K + H2O
?
-
cleavage occurs only in unactivated macrophages, m-calpain cleavage at Arg81-Gly82 generates the two selenoprotein K isoforms
-
-
?
SLLVY-7-amido-4-methylcoumarin + H2O
SLLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
succinyl-bovine serum albumin + H2O
?
-
-
-
-
?
succinyl-bovine-serum-albumin + H2O
?
-
-
-
-
?
succinyl-casein + H2O
?
-
-
-
-
?
succinyl-insulin B + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
succinyl-Leu-Met-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
succinyl-protamine + H2O
?
-
-
-
-
?
synaptotagmin-1 + H2O
?
-
-
-
-
?
t-Boc-Leu-Met-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butoxycarbonyl-Leu-Met + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
tert-butyloxycarbonyl-L-leucyl-L-methionine-7-amido-4-chloromethylcoumarin + H2O
tert-butyloxycarbonyl-L-leucyl-L-methionine + 7-amino-4-chloromethylcoumarin
-
-
-
-
?
TPLKSPPPSPR + H2O
?
-
efficient substrate
-
-
?
transgelin-3 + H2O
?
-
-
-
-
?
ubiquitin-activating enzyme E1 + H2O
?
-
-
-
-
?
upstream stimulatory factor + H2O
?
-
-
-
-
?
vimentin + H2O
?
-
-
-
-
?
voltage dependent anion channel + H2O
?
-
-
-
-
?
voltage-dependent anion channel + H2O
?
-
mitochondrial m-calpain truncates voltage-dependent anion channel in Ca2+-dependent manner
-
-
?
desmin + H2O
additional information
-
calmodulin-dependent protein kinase II deltaB + H2O
?
-
-
-
?
calmodulin-dependent protein kinase II deltaB + H2O
?
angiotensin II enhances the interaction between activated calpain-2 and Ca2+/calmodulin-dependent protein kinase II deltaB (CaMKIIdB), and promotes the degradation of CaMKIIdB by calpain-2 in the nuclei of hypertrophied cardiomyocytes. The depressed CaMKIIdeltaB downregulates the expression of antiapoptotic Bcl-2 leading to mitochondrial depolarization and release of cytochrome c which leads to apoptosis of hypertrophied cardiomyocytes
-
-
?
casein + H2O
?
-
-
-
-
?
crystallin + H2O
?
-
-
-
-
?
crystallin + H2O
?
-
alphaA crystallin in lenses from wild-type mice is proteolyzed by both calpain 2 and Lp82. Crystallins proteolyzed by calpain Lp82 are more susceptible to insolubilization than crystallins proteolyzed by calpain 2
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
-
GAP-43 cleavage at Ser41 residue in synaptosomes is mediated by m-calpain
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
-
a GAP-43 fragment, lacking about 40 N-terminal residues (named GAP-43-3), is produced by m-calpain. The fragment prevents complete cleavage of intact GAP-43 by m-calpain as a negative feedback
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
-
a GAP-43 fragment, lacking about 40 N-terminal residues (named GAP-43-3), is produced by m-calpain. The fragment prevents complete cleavage of intact GAP-43 by m-calpain as a negative feedback
-
-
?
IkappaBalpha + H2O
?
-
-
-
-
?
IkappaBalpha + H2O
?
-
a parallel pathway that degrades IkappaBalpha and activates NF-kappaB activation independently of the ubiquitin-proteasome pathway
-
-
?
MARCKS protein + H2O
?
MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney
-
-
?
MARCKS protein + H2O
?
MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+
-
-
?
myocillin + H2O
?
-
-
-
-
?
myocillin + H2O
?
-
calpain II is responsible for the intracellular processing of myocilin in the lumen of the endoplasmic reticulum. It is proposed that this cleavage might regulate extracellular interactions of myocilin, contributing to the control of intraocular pressure
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
-
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
calpain-2 activation cleaves striatal-enriched protein tyrosine phosphatase and activates STEP-mediated pro-death pathway in retinal ganglion cells after intraocular pressure elevation
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
talin + H2O
?
-
-
-
-
?
desmin + H2O
additional information
-
-
-
two proteolytic fragments of 35000 Da and of 16000 Da
?
additional information
?
-
-
no proteolysis of actin
-
-
?
additional information
?
-
-
the enzyme might be involved in light-dependent regulation of disk membrane morphogenesis by proteolysis of myosin II
-
-
?
additional information
?
-
-
fetuin A is a potential extracellular regulator of m-calpain at nascent sites of plasma membrane wounding
-
-
?
additional information
?
-
enzyme is involved in cytoskeleton remodelling and signal transduction
-
-
?
additional information
?
-
-
enzyme is involved in cytoskeleton remodelling and signal transduction
-
-
?
additional information
?
-
enzyme is involved in essential cellular functions mediated by calcium. Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit
-
-
?
additional information
?
-
-
enzyme plays a pivotal role during the earlier stages of myogenesis, particularly during fusion. MyoD and myogenin can transactivate capn2, but MyoD shows a higher transactivation level for the regulatory sequences
-
-
?
additional information
?
-
-
calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons
-
-
?
additional information
?
-
pathological conditions associated with the gene of calpain 2: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, Parkinson's disease, neurodegenerative disorders, cataracts, cancer
-
-
?
additional information
?
-
-
pathological conditions associated with the gene of calpain 2: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, Parkinson's disease, neurodegenerative disorders, cataracts, cancer
-
-
?
additional information
?
-
-
calpain 2activity is critical for the life cycle of echovirus 1 and important in the multiplication of the viral RNA genome
-
-
?
additional information
?
-
-
calpain mediates angiogenic effects induced by vascular endothelial growth factor by modulating actin cytoskeletal organization
-
-
?
additional information
?
-
-
calpain-2 plays an important role in lung endothelial cell migration and proliferation
-
-
?
additional information
?
-
-
catalytic activity of calpain is required to limit pseudopod formation in the direction of chemoattractant and for efficient chemotaxis. Calpain 2 is a novel component of the frontness signal that promotes polarization during chemotaxis
-
-
?
additional information
?
-
-
m-calpain activity is triggered by Ca2+-influx and promoted mainly through the phosphatidylinositol 3-kinase pathway
-
-
?
additional information
?
-
-
M-calpain is the major candidate of the proteinase to generate the aggrecan product with the COOH terminal neoepitope VPGVA709 (consisting of two NH2 terminal globular domain G1 and G2 and KS side chains) during the intracellular aggrecan processing
-
-
?
additional information
?
-
-
caspase-8 associates with calpain-2
-
-
?
additional information
?
-
-
epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway
-
-
?
additional information
?
-
-
calpain 2 is likely to be involved with signal transduction events in the lens
-
-
?
additional information
?
-
-
calpain 2 plays a role in limiting membrane protrusion and in regulating lamellipodial dynamics at the leading edge of migrating cells
-
-
?
additional information
?
-
-
functions for nCL-2 involve the membrane trafficking of mucus cells by interacting with coat proteins
-
-
?
additional information
?
-
-
CAPN2 may represent a key factor in development from the first cell division
-
-
?
additional information
?
-
m-calpain is vital for development of the preimplantation murine embryo
-
-
?
additional information
?
-
-
m-calpain is vital for development of the preimplantation murine embryo
-
-
?
additional information
?
-
-
the enzyme is involved in myoblast fusion by cleaving certain proteins. This cleavage could modify membrane and cytoskeleton organization for the myoblast to fuse
-
-
?
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
?
-
-
calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion contributes to cell death after myocardial ischemia
-
-
?
additional information
?
-
-
ERp75 plays important role in the refolding of mitochondrial m-calpain large subunit, cytosolic m-calpain does not associate with ERp57
-
-
?
additional information
?
-
-
representatives of the protein phosphatase 2A subunit classes C, PR65/A, PR55/B and PR61/B' are resistant to m-calpain-mediated degradation
-
-
?
additional information
?
-
enzyme is involved in myofibrillar protein degradation
-
-
?
additional information
?
-
-
enzyme is involved in myofibrillar protein degradation
-
-
?
additional information
?
-
hypoxia upregulates calpain activity and mRNA expression in pulmonary artery endothelial cells
-
-
?
vimentin + H2O
additional information
-
-
-
four proteolytic fragments: 3 major compounds of 54000 Da, 46000 Da and 20000 Da, and a minor fragment of 28000 Da
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-2 spectrin + H2O
?
-
-
-
-
?
alpha-spectrin + H2O
145000 Da fragment + ?
-
-
-
-
?
aminopeptidase B + H2O
?
-
-
-
-
?
androgen receptor + H2O
?
-
-
-
-
?
beta-transducin repeat containing protein + H2O
?
-
-
-
-
?
calmodulin-dependent protein kinase II deltaB + H2O
?
angiotensin II enhances the interaction between activated calpain-2 and Ca2+/calmodulin-dependent protein kinase II deltaB (CaMKIIdB), and promotes the degradation of CaMKIIdB by calpain-2 in the nuclei of hypertrophied cardiomyocytes. The depressed CaMKIIdeltaB downregulates the expression of antiapoptotic Bcl-2 leading to mitochondrial depolarization and release of cytochrome c which leads to apoptosis of hypertrophied cardiomyocytes
-
-
?
caspase-3 + H2O
?
-
-
-
-
?
collapsin response mediator protein-1 + H2O
?
-
collapsin response mediator protein-1 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-2 + H2O
?
-
collapsin response mediator protein-2 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-4 + H2O
?
-
collapsin response mediator protein-4 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-5 + H2O
?
-
-
-
-
?
cortactin + H2O
?
-
-
-
-
?
crystallin + H2O
?
-
alphaA crystallin in lenses from wild-type mice is proteolyzed by both calpain 2 and Lp82. Crystallins proteolyzed by calpain Lp82 are more susceptible to insolubilization than crystallins proteolyzed by calpain 2
-
-
?
dihydropteridine reductase + H2O
?
-
the dihydropteridine reductase 29000 Da subunit is cleaved just before the 35th Ser and the 48th Val residue from the N-terminus, generating two new fragments of 21000 Da and 19000 Da which are more active than the native enzyme
-
-
?
filamin A + H2O
?
-
-
-
-
?
frequenin homolog + H2O
?
-
-
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
-
GAP-43 cleavage at Ser41 residue in synaptosomes is mediated by m-calpain
-
-
?
heterogeneous nuclear ribonucleoprotein F + H2O
?
-
-
-
-
?
heterogeneous nuclear ribonucleoprotein K + H2O
?
-
-
-
-
?
IkappaBalpha + H2O
?
-
a parallel pathway that degrades IkappaBalpha and activates NF-kappaB activation independently of the ubiquitin-proteasome pathway
-
-
?
internexin + H2O
?
-
-
-
-
?
IP3R1 + H2O
?
-
in presence of Ca2þ, m-calpain cleaves IP3R1 in the endoplasmic lumen
-
-
?
laminin receptor 1 + H2O
?
-
-
-
-
?
mammalian actin-binding protein-1 + H2O
?
-
the preferred cleavage site occurs between the actin-binding domain and the proline-rich region, generating a C-terminal mAbp1 fragment
-
-
?
MARCKS protein + H2O
?
MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney
-
-
?
microtubule-associated protein 1B + H2O
?
-
-
-
-
?
myocillin + H2O
?
-
calpain II is responsible for the intracellular processing of myocilin in the lumen of the endoplasmic reticulum. It is proposed that this cleavage might regulate extracellular interactions of myocilin, contributing to the control of intraocular pressure
-
-
?
neurofilament + H2O
?
-
-
-
-
?
nucleolin + H2O
?
-
-
-
-
?
p35 + H2O
25000 Da fragment of p35 + ?
-
calpain-specific substrate
-
-
?
selenoprotein K + H2O
?
-
cleavage occurs only in unactivated macrophages, m-calpain cleavage at Arg81-Gly82 generates the two selenoprotein K isoforms
-
-
?
striatal-enriched protein tyrosine phosphatase + H2O
?
calpain-2 activation cleaves striatal-enriched protein tyrosine phosphatase and activates STEP-mediated pro-death pathway in retinal ganglion cells after intraocular pressure elevation
-
-
?
synaptotagmin-1 + H2O
?
-
-
-
-
?
transgelin-3 + H2O
?
-
-
-
-
?
ubiquitin-activating enzyme E1 + H2O
?
-
-
-
-
?
vimentin + H2O
?
-
-
-
-
?
additional information
?
-
casein + H2O
?
-
-
-
-
?
additional information
?
-
-
the enzyme might be involved in light-dependent regulation of disk membrane morphogenesis by proteolysis of myosin II
-
-
?
additional information
?
-
-
fetuin A is a potential extracellular regulator of m-calpain at nascent sites of plasma membrane wounding
-
-
?
additional information
?
-
enzyme is involved in cytoskeleton remodelling and signal transduction
-
-
?
additional information
?
-
-
enzyme is involved in cytoskeleton remodelling and signal transduction
-
-
?
additional information
?
-
enzyme is involved in essential cellular functions mediated by calcium. Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit
-
-
?
additional information
?
-
-
enzyme plays a pivotal role during the earlier stages of myogenesis, particularly during fusion. MyoD and myogenin can transactivate capn2, but MyoD shows a higher transactivation level for the regulatory sequences
-
-
?
additional information
?
-
-
calpain mediates calcium-induced activation of the Erk1,2 MAPK pathway and cytoskeletal phosphorylation in neurons
-
-
?
additional information
?
-
pathological conditions associated with the gene of calpain 2: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, Parkinson's disease, neurodegenerative disorders, cataracts, cancer
-
-
?
additional information
?
-
-
pathological conditions associated with the gene of calpain 2: muscular dystrophy, stroke, traumatic brain injury, spinal cord injury, Alzheimer's diseases, Parkinson's disease, neurodegenerative disorders, cataracts, cancer
-
-
?
additional information
?
-
-
calpain 2activity is critical for the life cycle of echovirus 1 and important in the multiplication of the viral RNA genome
-
-
?
additional information
?
-
-
calpain mediates angiogenic effects induced by vascular endothelial growth factor by modulating actin cytoskeletal organization
-
-
?
additional information
?
-
-
calpain-2 plays an important role in lung endothelial cell migration and proliferation
-
-
?
additional information
?
-
-
catalytic activity of calpain is required to limit pseudopod formation in the direction of chemoattractant and for efficient chemotaxis. Calpain 2 is a novel component of the frontness signal that promotes polarization during chemotaxis
-
-
?
additional information
?
-
-
m-calpain activity is triggered by Ca2+-influx and promoted mainly through the phosphatidylinositol 3-kinase pathway
-
-
?
additional information
?
-
-
M-calpain is the major candidate of the proteinase to generate the aggrecan product with the COOH terminal neoepitope VPGVA709 (consisting of two NH2 terminal globular domain G1 and G2 and KS side chains) during the intracellular aggrecan processing
-
-
?
additional information
?
-
-
epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway
-
-
?
additional information
?
-
-
calpain 2 is likely to be involved with signal transduction events in the lens
-
-
?
additional information
?
-
-
calpain 2 plays a role in limiting membrane protrusion and in regulating lamellipodial dynamics at the leading edge of migrating cells
-
-
?
additional information
?
-
-
functions for nCL-2 involve the membrane trafficking of mucus cells by interacting with coat proteins
-
-
?
additional information
?
-
-
CAPN2 may represent a key factor in development from the first cell division
-
-
?
additional information
?
-
m-calpain is vital for development of the preimplantation murine embryo
-
-
?
additional information
?
-
-
m-calpain is vital for development of the preimplantation murine embryo
-
-
?
additional information
?
-
-
the enzyme is involved in myoblast fusion by cleaving certain proteins. This cleavage could modify membrane and cytoskeleton organization for the myoblast to fuse
-
-
?
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
?
-
-
calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion contributes to cell death after myocardial ischemia
-
-
?
additional information
?
-
-
ERp75 plays important role in the refolding of mitochondrial m-calpain large subunit, cytosolic m-calpain does not associate with ERp57
-
-
?
additional information
?
-
enzyme is involved in myofibrillar protein degradation
-
-
?
additional information
?
-
-
enzyme is involved in myofibrillar protein degradation
-
-
?
additional information
?
-
hypoxia upregulates calpain activity and mRNA expression in pulmonary artery endothelial cells
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Al3+
-
millimolar concentrations of Al3+ activate at at submillimolar concentrations of Ca2+
K+
-
5 mM, activates in presence of 5 mM Ca2+
Na+
-
5 mM, activates in presence of 5 mM Ca2+
Ba2+
-
activates
Ba2+
-
1 mM, decreases the Ca2+-requirement for maximal activity from 0.4 mM to 0.3 mM. Synergistic activating effect with Ca2+
Ba2+
-
5 mM 85.4% of the activation with 5 mM Ca2+
Ca2+
-
requires approximately 0.3 mM Ca2+ for half-maximal activity in vivo
Ca2+
-
half maximal activity for retina and brain enzyme is 0.262 mM and 0.311 mM, maximal activity near 1 mM, no activity in presence of 0.03 mM
Ca2+
-
optimum activity at 5 mM Ca2+
Ca2+
-
treatment of the endoplasmic reticulum with Ca2+ (5 mM) dissociates m-calpain-calpastatin association leading to the activation of m-calpain
Ca2+
-
best activator at 2.5 mM, maximal caseinolytic activity at 2.2 mM, half-maximal caseinolytic activity at 0.312 mM
Ca2+
-
half-maximal activity at 0.18 mM
Ca2+
-
required for activity
Ca2+
-
0.4 mM Ca2+ is required for 50% caseinolysis of recombinant enzyme
Ca2+
-
calcium-dependent cysteine protease
Ca2+
-
calpain 2 is activated with addition of CaCl+ to 1 mM
Ca2+
-
requires millimolar calcium concentrations for activation
Ca2+
-
requires millimolar order calcium ions for activation
Ca2+
-
half-maximal activation at 0.8 mM, maximal activation at 1.5 mM
Ca2+
-
half-maximal activity at 0.4 mM, maximal activity at 1.5 mM
Ca2+
-
half-maximal activity at 2.4 mM, maximal activity at 5 mM
Ca2+
-
absolute requirement
Ca2+
-
required for activity
Ca2+
-
half-maximal activation at 0.5 mM
Ca2+
half-maximal activity of wild-type enzyme at 0.242 mM
Ca2+
-
Kd-value: 0.325 mM. 25% of the difference in Kd values between mu-calpain 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+
Ca2+-binding must induce conformational changes that reorient the protease domains to form a functional active site
Ca2+
-
wild-type enzyme has a Kd-value of 0.325 mM
Ca2+
-
half-maximal activation at 0.2 mM, full activity at 1 mM
Ca2+
activates. The results support the hypothesis that Ca2+ induces movement of domains I and II closer together to form the functional active site of calpain
Ca2+
half-maximal activity is 0.242 mM for wilde-type enzyme, 0.129 mM for the E504S mutant, 0.226 mM for the K226S mutant, 0.261 mM for the K230S mutant, 0.183 mM for the K234 mutant, 0.256 mM for the K230E mutant and 0.159 mM for the K234E mutant
Ca2+
-
Ca2+ induces calpain translocation to the membrane during ischemia
Ca2+
-
Ca2+-induced calpain translocation to the membrane during ischemia is independent of its activation
Ca2+
-
the Ca2+ dependency of mitochondrial m-calpain is similar to that of cytosolic m-calpain, 1 mM Ca2+ activates.
Ca2+
-
3 mM used in assay conditions
Ca2+
-
maximum calcium requirement of 0.6 mM
Ca2+
-
5 mM required for optimal activity
Ca2+
-
required for activity
Ca2+
-
half-maximal activation at 0.2 mM, maximal activation at 1 mM
Ca2+
-
half-maximal activation at 0.15 mM, maximal activation at 1 mM
Ca2+
-
half-maximal activity at 0.23 mM, maximal activity at 1-2.5 mM
Mg2+
-
1 mM decreases the Ca2+-requirement for maximal activity from 0.4 mM to 0.3 mM. Synergistic activating effect with Ca2+
Mg2+
-
5 mM, activates in presence of 5 mM Ca2+
Mn2+
-
activates
Mn2+
-
1 mM, decreases the half-maximal Ca2+-requirement from 0.4 mM to 0.1 mM, decreases the Ca2+-requirement for maximal activity from 1.5 mM to 1 mM
Mn2+
-
5 mM 73.6% of the activation with 5 mM Ca2+. Synergistic activating effect with Ca2+
Sr2+
-
2.5 mM, 66% of the activation obtained with Ca2+, maximal caseinolytic activity at 5.9 mM, half-maximal caseinolytic activity at 1.886 mM. Autolysis in presence of 5 mM Ca2+. The 80000 Da subunit is rapidly autolyzed in two smaller bands of 73000 Da and 69000 Da. The small subunit of 24000 da is degraded into three bands of 22000 Da, 19300 Da and 17800 Da. It is not clear whether autolysis is necessary for calpain to become proteolytically active
Sr2+
-
activates, Ka: 5.1 mM
Sr2+
-
1 mM, decreases the half-maximal Ca2+-requirement from 0.4 mM to 0.1 mM, decreases the Ca2+-requirement for maximal activity from 1.5 mM to 1 mM. Synergistic activating effect with Ca2+
Sr2+
-
5 mM 91% of the activation with 5 mM Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S)-3-phenyl-2-([[(2S)-1-(phenylsulfonyl)pyrrolidin-2-yl]carbonyl]amino)propanoic acid
-
-
(2S)-4-methyl-2-[(phenylsulfonyl)amino]pentanoic acid
-
-
(2S,3S)-trans-epoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester
-
0.01 mM, 50% inhibition
1,2-bis(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid tetra(acetoxymethyl) ester
-
-
110 kDa calpastatin
-
-
-
3,4-dichloroisocoumarin
-
0.05 mM, 11% inhibition
4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid
-
5 mM, 23% inhibition
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-NH2
-
-
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
-
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-Pro-Arg-NH2
-
-
Ac-Thr-Ser-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
-
Ac-Thr-Trp-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
-
acetyl-Leu-Leu-Met-CHO
-
selectively inhibits the activity of calpain-2
Al3+
-
inactivation at millimolar concentration of Ca2+
alpha2-Macroglobulin
-
0.05 mg/ml, 11% inhibition
-
benzyloxycarbonyl-L-leucyl-L-leucinal
-
-
benzyloxycarbonyl-Leu-Abu-CONH-CH2-C6H3(3,5-(OMe)2)
calpain-2 selective inhibitor. A selective calpain-2 inhibitor could prevent acute glaucoma-induced retinal ganglion cell death and blindness
benzyloxycarbonyl-Leu-Leu-leucinal
-
-
benzyloxycarbonyl-Leu-Leu-phenylalaninal
-
-
benzyloxycarbonyl-Leu-Leu-Tyr diazomethyl ketone
-
-
benzyloxycarbonyl-Leu-norleucinal
-
-
benzyloxycarbonyl-LLY-fluoromethylketone
-
-
Ca2+
initiation of autolysis of calpain 2 by adding of 1 mM CaCl2
Calmidazolium
-
calpain-specific inhibitor
Cbz-Leu-DL-Abu-CONH-(CH2)3-(4-methylpiperazin-1-yl)
-
-
Cbz-Leu-DL-Abu-CONH-(CH2)3-2-methoxyadenin-9-yl
-
-
Cbz-Leu-DL-Abu-CONH-(CH2)3-adenin-9-yl
-
-
Cbz-Leu-DL-Abu-CONH-(CH2)3-cytosin-3-yl
-
-
Cbz-Leu-DL-Abu-CONH-(CH2)3-morpholine
-
-
CBZ-Leu-DL-Phe-CONH-(CH2)2-N-(CH3)2
-
-
CBZ-Leu-DL-Phe-CONH-(CH2)3-(4-methylpiperazin-1-yl)
-
-
CBZ-Leu-DL-Phe-CONH-(CH2)3-2-methoxyadenin-9-yl
-
-
CBZ-Leu-DL-Phe-CONH-(CH2)3-adenin-9-yl
-
best inhibitor
CBZ-Leu-DL-Phe-CONH-(CH2)3-cytosin-3-yl
-
-
CBZ-Leu-DL-Phe-CONH-(CH2)3-N-(CH3)2
-
-
E-64c
-
0.01 mM, 80-90% inhibition
Ep-475
-
0.001 mM, 49% inhibition of the enzyme from retina, 46% inhibition of the enzyme from brain
ethyl N-(phenylsulfonyl)-L-leucyl-L-phenylalaninate
-
-
iodoacetamide
-
1 mM, 64% inhibition
Mg2+
-
5 mM, inhibits in presence of 5 mM Ca2+
N-acetyl-L-leucyl-L-leucyl-L-methioninal
-
-
N-tosyl-Lys-chloromethyl ketone
-
0.5 mM, 69% inhibition
N-tosyl-Phe-chloromethyl ketone
-
0.5 mM, 91% inhibition
NaCl
-
m-calpain is more active at 165 mM NaCl than at 295 mM NaCl
pepstatin
-
0.01 mM, 99% inhibition
pepstatin A
-
1 mM, 60-80% inhibition
PMSF
-
1 mM, 6% inhibition
Polyethylene glycol
-
PEG-4000, PEG-100000 or PEG-20000, inhibition at concentrations higher than 0.5%
protease inhibitor
-
0.002 mg/ml, 6% inhibition
-
Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-Pro-Arg-NH2
-
-
TLCK
-
0.1 mM, 60-80% inhibition
Z-Val-Phe-CHO
-
i.e. MDL-28710m, 1.0 microM
acetyl-Leu-Leu-Nle-CHO
-
complete inhibition at 0.001 mM
acetyl-Leu-Leu-Nle-CHO
-
broad spectrum calpain inhibitor
acetyl-Leu-Leu-Nle-CHO
-
-
ALLM
-
-
antipain
-
0.05 mM, complete inhibition
antipain
-
0.01 mM, 80-90% inhibition
antipain
-
0.01 mM 56% inhibition
antipain
-
0.02 mM, 82% loss of activity
antipain
-
0.02 mM, 87% loss of activity
calpain inhibitor I
-
0.05 mM, 99% inhibition
calpain inhibitor I
-
0.002 mM, 95% loss of activity
calpain inhibitor I
-
0.002 mM, 90% loss of activity
calpain inhibitor II
-
0.05 mM, complete inhibition
calpain inhibitor II
-
0.002 mM, 67% loss of activity
calpain inhibitor II
-
0.002 mM, 93% loss of activity
calpastatin
-
specific competitive inhibitor
-
calpastatin
-
specific inhibitor
-
calpastatin
-
endogenous inhibitor
-
calpastatin
-
endogenous inhibitor
-
calpastatin
-
endogenous inhibitor
-
calpastatin
-
endogenous inhibitor of calpain
-
calpastatin
-
inhibition of m-calpain is greater at pH 7.5 than at pH 6.5 at both 165 mM and 295 mM NaCl. Percentage inhibition is greater at 295 mM than at 165 mM NaCl
-
calpastatin
-
oxidation lowers calpastatin inhibition of m-calpain at al pH and ionic strength combinations
-
calpeptin
-
50% inhibition of maximal caseinolytic activity at 10 nM and 21 nM for retinal and brain calpain
calpeptin
-
complete inhibition at 0.001 mM
calpeptin
-
Z-Leu-Nle-CHO
Cd2+
-
5 mM, completely blocks activation of the enzyme by Ca2+
Cd2+
-
5 mM, inhibits in presence of 5 mM Ca2+
Co2+
-
2.5 mM, strong
Co2+
-
5 mM, completely blocks activation of the enzyme by Ca2+
Co2+
-
5 mM, inhibits in presence of 5 mM Ca2+
Cu2+
-
5 mM, completely blocks activation of the enzyme by Ca2+
Cu2+
-
5 mM, inhibits in presence of 5 mM Ca2+
E-64
-
0.01 mM, 98% inhibition
E-64
-
i.e. trans-epoxysuccinyl-L-leucylamido-(4-guanido)butane
E-64
-
0.01 mM 89% inhibition
E-64
-
0.05 mg/ml, complete inhibition
EDTA
-
5 mM, complete inhibition
EDTA
-
completely inactivated by 4 mM EDTA plus 4 mM EGTA
EGTA
-
-
EGTA
-
completely inactivated by 4 mM EDTA plus 4 mM EGTA
Fe2+
-
2.5 mM, strong
Fe2+
-
5 mM, inhibits in presence of 5 mM Ca2+
Fe3+
-
2.5 mM, complete
GAP-43-3
-
a GAP-43 fragment, lacking about 40 N-terminal residues (named GAP-43-3), is produced by m-calpain-mediated cleavage of GAP-43. The fragment prevents complete cleavage of intact GAP-43 by m-calpain as a negative feedback. GAP-43-3 also blocks m-calpain activity against casein
-
GAP-43-3
-
a GAP-43 fragment, lacking about 40 N-terminal residues (named GAP-43-3), is produced by m-calpain-mediated cleavage of GAP-43. The fragment prevents complete cleavage of intact GAP-43 by m-calpain as a negative feedback. GAP-43-3 also blocks m-calpain activity against casein
-
Hg2+
-
2.5 mM, complete
Hg2+
-
5 mM, inhibits in presence of 5 mM Ca2+
iodoacetic acid
-
0.1 mM, 99% inhibition
iodoacetic acid
-
1 mM, 76% inhibition
iodoacetic acid
-
1 mM, complete loss of activity
iodoacetic acid
-
1 mM, 99% loss of activity
K+
-
inhibits at high concentrations
K+
-
5 mM, inhibits in presence of 5 mM Ca2+
leupeptin
-
0.001 mM, 67% inhibition of enzyme from retina and brain
leupeptin
-
0.05 mM, 99% inhibition
leupeptin
-
0.01 mM, 80-90% inhibition
leupeptin
-
0.01 mM 85% inhibition
leupeptin
-
0.002 mM, complete loss of activity
leupeptin
-
0.05 mg/ml, complete inhibition
leupeptin
-
0.002 mM, 93% loss of activity
MDL28170
-
-
MDL28170
-
selective calpain inhibitor
Na+
-
inhibits at high concentrations
Na+
-
5 mM, inhibits in presence of 5 mM Ca2+
NEM
-
5 mM, complete inhibition
NEM
-
1 mM, 93% inhibition
NEM
-
3.0 mM, high inhibition of activity in presence or absence of Ca2+
Ni2+
-
2.5 mM, complete
Ni2+
-
5 mM, completely blocks activation of the enzyme by Ca2+
Ni2+
-
5 mM, inhibits in presence of 5 mM Ca2+
PCMB
-
5 mM, 24% inhibition
PCMB
-
1 mM, 56% inhibition
PCMB
-
1 mM, 42% inhibition
PD150606
-
-
Zn2+
-
2.5 mM, complete
Zn2+
-
5 mM, completely blocks activation of the enzyme by Ca2+
Zn2+
-
5 mM, inhibits in presence of 5 mM Ca2+
additional information
-
suppression of calpain-2 expression with adenovirus vector-mediated RNAi
-
additional information
-
specific capn2 shRNA reduces expression of the targeted isoform
-
additional information
-
not inhibited by benzyloxycarbonyl-VAD-fluoromethylketone
-
additional information
-
not inhibited by Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-NH2, Ac-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Thr-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Ser-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Gln-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Val-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2, Ac-Thr-Pro-Leu-alpha-azaglycine-Thr-Pro-Pro-Pro-Ser-NH2, and Ac-Thr-Pro-Leu-alpha-azaglycine-Arg-Pro-Pro-Pro-Ser-NH2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.5
Boc-Val-Leu-Lys-methylcoumarin
-
pH 7.5, room temperature
2.2
succinyl-bovine serum albumin
-
pH 7.5, 25°C
-
10
succinyl-casein
-
pH 7.5, 25°C
-
453.7
succinyl-insulin B
-
pH 7.5, 25°C
-
0.459 - 0.461
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
19.32
succinyl-Leu-Leu-Val-Tyr-methylcoumarin
-
pH 7.5, room temperature
4.66 - 4.68
succinyl-Leu-Met-7-amido-4-methylcoumarin
0.431 - 3.18
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
101.3
succinyl-protamine
-
pH 7.5, 25°C
-
5.33
t-Boc-Leu-Met-methylcoumarin
-
pH 7.5, room temperature
8.11 - 8.12
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
0.459
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.461
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
4.66
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
4.68
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.431
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
-
2.1
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
2.13
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
3.18
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
pH 7.5, room temperature
8.11
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
8.12
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.341
Boc-Val-Leu-Lys-methylcoumarin
-
pH 7.5, room temperature
0.062 - 0.063
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
0.0394
succinyl-Leu-Leu-Val-Tyr-methylcoumarin
-
pH 7.5, room temperature
0.186 - 0.189
succinyl-Leu-Met-7-amido-4-methylcoumarin
0.04 - 0.084
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
0.546
t-Boc-Leu-Met-methylcoumarin
-
-
1.06 - 1.08
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
0.062
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.063
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.186
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.189
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.04
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
pH 7.5, room temperature
0.083
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.084
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
1.06
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
1.08
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
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0.135 - 0.137
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
0.0399 - 0.0404
succinyl-Leu-Met-7-amido-4-methylcoumarin
0.0394 - 0.0395
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
0.131 - 0.133
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
0.135
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.137
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.0399
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.0404
succinyl-Leu-Met-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.0394
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.0395
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.131
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum membrane m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
0.133
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
endoplasmic reticulum lumen m-calpain, in 100 mM imidazole-HCl buffer (pH 7.5), 5 mM L-cysteine, 2.5 mM 2-mercaptoethanol, 5 mM CaCl2, and 4% (v/v) dimethyl sulfoxide, at 30°C
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0.0898
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0087
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0072
Ac-Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-Pro-Arg-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0035
Ac-Thr-Ser-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.0058
Ac-Thr-Trp-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
0.00206
antipain
-
room temperature, pH 7.5, with succinyl-Met-Leu-methylcoumarin as substrate
0.000286
Cbz-Leu-DL-Abu-CONH-(CH2)3-(4-methylpiperazin-1-yl)
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000077
Cbz-Leu-DL-Abu-CONH-(CH2)3-2-methoxyadenin-9-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00007
Cbz-Leu-DL-Abu-CONH-(CH2)3-adenin-9-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00114
Cbz-Leu-DL-Abu-CONH-(CH2)3-cytosin-3-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000041
Cbz-Leu-DL-Abu-CONH-(CH2)3-morpholine
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00352
CBZ-Leu-DL-Phe-CONH-(CH2)2-N-(CH3)2
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00636
CBZ-Leu-DL-Phe-CONH-(CH2)3-(4-methylpiperazin-1-yl)
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000209
CBZ-Leu-DL-Phe-CONH-(CH2)3-2-methoxyadenin-9-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000068
CBZ-Leu-DL-Phe-CONH-(CH2)3-adenin-9-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000438
CBZ-Leu-DL-Phe-CONH-(CH2)3-cytosin-3-yl
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.000844
CBZ-Leu-DL-Phe-CONH-(CH2)3-N-(CH3)2
-
in 50 mM Tris-HCl, 50 mM NaCl, 1 mM EDTA, 1 mM EGTA, 0.1% CHAPS, pH 7.5, 10 mM dithiothreitol, 5 mM CaCl2, and less than 5% (v/v) DMSO, temperature not specified in the publication
0.00092
leupeptin
-
room temperature, pH 7.5, with succinyl-Met-Leu-methylcoumarin as substrate
0.0203
Thr-Pro-Leu-alpha-azaglycine-Ser-Pro-Pro-Pro-Ser-Pro-Arg-NH2
-
in 10 mM HEPES, 150 mM NaCl, 1 mM EDTA, pH 7.5, at 22°C
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malfunction
-
calpain 2 depletion impairs mitosis and induces apoptosis, low Capn2 levels induce chromosome alignment defects, the loss of histone H3 threonine 3 phosphorylation at centromeres, and premature sister chromatid separation
malfunction
-
calpain inhibition blocks the increased colonic epithelial cell invasion caused by NM IIA knockdown
malfunction
-
in vivo knockdown of calpain2 disrupts metastasis among apoptosis-resistant tumors
malfunction
-
inhibition of m-calpain induces expression of the adult alpha- and beta-globin genes
malfunction
-
short interfering RNA-induced silencing of m-calpain results in increased RhoA activity and hyperpermeability in the aortic arch, which is accompanied by ROCK inhibitor-sensitive phosphorylation of downstream effecter LIM kinase 2, stress fibre accumulation in endothelium and enhanced interendothelial gaps
malfunction
-
the blockage of calpain 2 suppresses p38 MAPK phosphorylation
malfunction
-
inhibition of calpain activity limits cell migration and in vitro wound healing of IEC-6 cells
malfunction
-
knockdown of calpain 2 expression or chemical inhibition of calpain activity reduces glioblastoma cell invasion by 90%. Decreased expression of calpain 2 does not influence morphology or migration
malfunction
-
knockdown of calpain 2 inhibits T cell migration at both the level of single cell tracking and general cell speed
malfunction
-
calpain 2 knockdown in breast cancer cells correlates with reduced in vitro proliferation, migration, and in vivo tumorigenicity as well as reduced Akt activation, increased nuclear FoxO localization, and increased p27Kip1 expression
malfunction
-
calpain inhibition favors differentiation of neuronal stem cells. Calpain 2 silencing elicits decreased levels of glial fibrillary acidic protein
malfunction
-
knockdown of calpain 2 results in a 2.9fold decrease in the invasion of human glioblastoma cells in zebrafish brain. Calpain 2 knockdown cells demonstrate a 2.3fold lower area of dispersal compared with control cells
malfunction
-
the knockdown of calpain 2 significantly reduces cord formation, adhesion, and migration of human lymphatic microvascular dermal-derived endothelial cells on Matrigel compared to the control
metabolism
-
calpain 2 regulates endothelial nitric oxide synthase phosphorylation during cord formation by lymphatic endothelial cells on Matrigel
metabolism
isoform-specific hyperactivation of calpain-2, but not calpain-1 occurs at the synapse early in the pathogenesis of Alzheimer's disease potentially contributing to the deregulation of synaptic signaling in Alzheimer's disease
metabolism
MARCKS protein i.e. myristoylated alanine-rich C kinase substrate is a substrate of calpain-2 in the presence of Ca2+. Calpain-2 proteolysis of MARCKS promotes its interaction with lipids and ENaC at the plasma membrane to allow for the phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent regulation of epithelial sodium channel (ENaC) activity in the kidney
metabolism
nuclear translocation of calpain-2 mediates apoptosis of hypertrophied cardiomyocytes in transverse aortic constriction rat. Angiotensin II enhances the interaction between activated calpain-2 and Ca2+/calmodulin-dependent protein kinase II deltaB (CaMKIIdB), and promotes the degradation of CaMKIIdB by calpain-2 in the nuclei of hypertrophied cardiomyocytes. The depressed CaMKIIdeltaB downregulates the expression of antiapoptotic Bcl-2 leading to mitochondrial depolarization and release of cytochrome c which leads to apoptosis of hypertrophied cardiomyocytes
physiological function
-
an endoplasmic reticulum stress-related calpain-down-regulated PPAR-gamma/HO-1 pathway is involved in the interleukin-13-enhanced activated death of microglia
physiological function
-
Ca2+ overload induces apoptosis, which was correlated with calpain-2 activation
physiological function
-
calpain 2 activation is an early event in heat stress-induced male germ cell apoptosis
physiological function
-
calpain 2 is required for sister chromatid cohesion
physiological function
-
calpain 2 plays a role in the generation of the low molecular weight-androgen receptor in CWR22-R1 cells
physiological function
-
calpain 2 proteolysis of mAbp1 negatively regulates dorsal ruffle formation
physiological function
-
calpain 2-mediated proteolysis of focal adhesion kinase regulates adhesion dynamics in motile cells
physiological function
-
calpain-2 is crucial for promotion of migration and metastasis by caspase-8
physiological function
-
calpain-2 is involved in cell motility
physiological function
-
m-calpain antagonizes RhoA overactivation and endothelial barrier dysfunction under disturbed shear conditions
physiological function
-
m-calpain translocates during ischemia and activates at reperfusion in isolated rat hearts
physiological function
-
m-calpain up-regulates alpha- and beta-actin in alveolar rhabdomyosarcoma cells
physiological function
-
mitochondrial m-calpain is associated with ERp75 and plays an important role in releasing of truncated apoptosis-inducing factor from mitochondria
physiological function
-
mitochondrial m-calpain plays a role in the release of truncated apoptosis-inducing factor from the mitochondria by cleaving voltage-dependent anion channel
physiological function
-
calpain 2 controls turnover of lymphocyte function-associated antigen-1 adhesions on migrating T lymphocytes
physiological function
-
calpain 2 is required for matrix metalloproteinase-2 activity in glioblastoma cells. Calpain 2 is required for glioblastoma cell invasion, but not migration
physiological function
-
calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes
physiological function
-
the Ca2+-dependent release of m-calpain from the mitochondrial outer membrane has important implications in facilitating apoptotic cell death
physiological function
-
calpain 2 is involved in glial differentiation
physiological function
-
calpain 2 is required for the invasion of glioblastoma cells in the living zebrafish brain microenvironment
physiological function
-
calpain 2 promotes proliferation of cancer cells through Akt-FoxO-p27Kip1 signaling
physiological function
calpain-1 and calpain-2 play opposite functions in both synaptic plasticity/learning and memory and neuroprotection/neurodegeneration. Calpain-1 activation is necessary for certain forms of synaptic plasticity and learning and memory, while calpain-2 activation during a brief consolidation period limits the extent of plasticity/learning. Calpain-1 is neuroprotective, while calpain-2 is neurodegenerative. Calpain-2 activation, through the selective degradation of phosphatase PTEN, is linked to the regulation of mTOR-mediated local protein synthesis
physiological function
calpain-1 and calpain-2 play opposite roles in retinal ganglion cell death induced by acute intraocular pressure elevation. Calpain-1 activity supports survival of retinal ganglion cell after intraocular pressure elevation. Calpain-2 activity promotes cell death of retinal ganglion cells after intraocular pressure elevation. Calpain-2 activation cleaves striatal-enriched protein tyrosine phosphatase and activates STEP-mediated pro-death pathway in retinal ganglion cells after intraocular pressure elevation
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20000
-
1 * 74000 + 1 * 20000, SDS-PAGE
24000
-
1 * 80000 + 1 * 24000, SDS-PAGE
25000
-
1 * 80000 + 1 * 25000, SDS-PAGE
29000
-
1 * 80000 + 1 * 29000, SDS-PAGE
30000
-
1 * 80000 + 1 * 30000
32000
-
1 * 80000 + 1 * 32000, only the 80000 Da subunit shows catalytic ativity, SDS-PAGE
74000
-
1 * 74000 + 1 * 20000, SDS-PAGE
78000
-
1 * 78000 + 1 * 28000, SDS-PAGE
79920
-
m-calpain large subunit, calculated from amino acid sequence
8000
-
1 * 8000 + 1 * 28000, gel filtration, the endoplasmic reticulum membrane m-calpain containing 80000 Da large and 28000 Da small subunit is non-phosphorylated
84000
-
x * 84000, SDS-PAGE
110000
-
gel filtration
21000
-
1 * 80000 + 1 * 21000
21000
1 * 80000 + 1 * 21000, SDS-PAGE
28000
-
1 * 80000 + 1 * 28000, SDS-PAGE
28000
-
1 * 80000 + 1 * 28000, SDS-PAGE
28000
-
1 * 80000 + 1 * 28000, SDS-PAGE
28000
-
1 * 80000 + 1 * 28000, SDS-PAGE
28000
-
1 * 78000 + 1 * 28000, SDS-PAGE
28000
-
1 * 8000 + 1 * 28000, gel filtration, the endoplasmic reticulum membrane m-calpain containing 80000 Da large and 28000 Da small subunit is non-phosphorylated
58000
-
active form, SDS-PAGE
58000
-
x * 58000, active form, SDS-PAGE
80000
-
catalytic subunit, SDS-PAGE
80000
-
subunit, SDS-PAGE
80000
-
2 * 80000, SDS-PAGE
80000
-
x * 80000, SDS-PAGE
80000
-
x * 80000, SDS-PAGE
80000
-
1 * 80000 + 1 * 25000, SDS-PAGE
80000
-
1 * 80000 + 1 * 28000, SDS-PAGE
80000
-
1 * 80000 + 1 * 28000, SDS-PAGE
80000
-
1 * 80000 + 1 * 28000, SDS-PAGE
80000
-
1 * 80000 + 1 * 28000, SDS-PAGE
80000
-
1 * 80000 + 1 * 24000, SDS-PAGE
80000
-
1 * 80000 + 1 * 29000, SDS-PAGE
80000
-
1 * 80000 + 1 * 32000, only the 80000 Da subunit shows catalytic ativity, SDS-PAGE
80000
-
1 * 80000 + 1 * 21000
80000
-
1 * 80000 + 1 * 30000
80000
1 * 80000 + 1 * 21000, SDS-PAGE
80000
-
1 * 80000 + 1 * ?, SDS-PAGE
80000
-
x * 80000, inactive form, SDS-PAGE
80000
-
x * 80000, large subunit of m-calpain, SDS-PAGE
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C105S
-
mutant enzyme of mutant large subunit m-C105S-80K, coexpressed with 30000 Da subunit in Sf-9 cells does not degrade casein nor the artificial substrate succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide. The mutant enzyme does not show autolytic activity with Ca2+
K390R
-
overexpression of K390R mutant fails to increase the calpain activity since sumoylation at K390 is important for calpain-2 activity
D346E
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
D362K
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
G423R
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
H262A
inactive mutant enzyme
K225S
mutation decreases specific activity to 88% compared to wild-type enzyme
K226S
Ca2+ concentration required for half-maximal activity is 0.226 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K234E
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme
K234W
Ca2+ concentration required for half-maximal activity is 0.159 mM compared to 0.242 mM for the wild-type enzyme
N286A
inactive mutant enzyme
N286D
mutant enzyme with low activity
R417W
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
R628Q
mutant with decreased enzymatic activity
S369D
-
inactive mutant enzyme
S50D
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
S50E
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
S67E
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
T344M
mutant with decreased enzymatic activity, increased rate of autoproteolytic degradation
T370E
-
inactive mutant enzyme
T70E
-
mutant enzyme has the same specific activity and Ca2+ requirement as the wild-type enzyme
W288Y
mutant enzyme with low activity
C105S
inactive mutant enzyme
C105S
-
inactive mutant enzyme. The mutant enzyme provides a purified calpain, that is stable to autolysis and oxidation, which is likely to facilitate crystallization in both the presence and absence of calcium
E504S
Ca2+ concentration required for half-maximal activity is 0.129 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
E504S
mutation decreases specific activity to 90% compared to wild-type enzyme
K230E
Ca2+ concentration required for half-maximal activity is 0.256 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K230E
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme
K230S
Ca2+ concentration required for half-maximal activity is 0.261 mM compared to 0.242 mM for the wild-type enzyme
K230S
mutation has no significant effect on specific activity
K234S
Ca2+ concentration required for half-maximal activity is 0.183 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme
K234S
mutation decreases specific activity to 81% compared to wild-type enzyme
additional information
used as a model for calpain 3 in combination with calpastatin-inhibited rat calpain 2
additional information
-
replacement of the five m-calpain residues 517-521, Glu-Ala-Asn-Ile-Glu by the corresponding six mu-calpain residues 528-533, Gln-Ala-Asn-Leu-Pro-Asp, replacement of three m-calpain residues 639-641, Pro-Cys-Gln, by the corresponding three mu-calpain residues 651-653, Asn-Lys-Lys, or replacement of two m-calpain residues 578-579, Lys-Ile by the corresponding mu-calpain residues 590-591, Arg-Ser. Mutations do not affect the expression and Kd values of the resultant calpains. In a series of hybrid mu/m large-subunit calpains, the Kd values decrease progressively towards that of mu-calpain as the portion of mu-type sequence increases from 0 to 90%
additional information
used as a model for calpain 3 in combination with calpastatin-inhibited rat calpain 2
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