Information on EC 3.4.22.53 - calpain-2

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The expected taxonomic range for this enzyme is: Opisthokonta

EC NUMBER
COMMENTARY hide
3.4.22.53
-
RECOMMENDED NAME
GeneOntology No.
calpain-2
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
broad endopeptidase specificity
show the reaction diagram
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase; peptides, endopeptidase
-
CAS REGISTRY NUMBER
COMMENTARY hide
702693-80-9
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78990-62-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
Atlantic halibut
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Tilapia nilotica * Tilapia aurea
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
calpain 2 regulates endothelial nitric oxide synthase phosphorylation during cord formation by lymphatic endothelial cells on Matrigel
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AIF + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-2 spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-actin + H2O
?
show the reaction diagram
-
slow degradation
-
-
?
alpha-adaptin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-fodrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-neoendorphin + H2O
?
show the reaction diagram
-
cleavage of the 6Arg-7Lys bond
-
-
?
alpha-spectrin + H2O
145000 Da fragment + ?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-Tubulin + H2O
?
show the reaction diagram
-
complete digestion of alpha-tubulin with little effect on beta-tubulin
-
-
?
aminopeptidase B + H2O
?
show the reaction diagram
-
-
-
-
?
androgen receptor + H2O
?
show the reaction diagram
-
-
-
-
?
androgen receptor + H2O
low molecular weight androgen receptor + ?
show the reaction diagram
-
-
-
-
?
Angiotensin + H2O
?
show the reaction diagram
-
clevage of the 4tyr-5Ile bond
-
-
?
Bcl-xL + H2O
?
show the reaction diagram
-
-
-
-
?
benzoyl-Arg p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
beta-lipotropin(61-91) + H2O
?
show the reaction diagram
-
cleavage of the bonds: Thr76-Leu77, Lys84-Asn85 and Lys88-Lys89
-
-
?
beta-neoendorphin + H2O
?
show the reaction diagram
-
cleavage of the 6Arg-7Lys bond
-
-
?
beta-subunit of coatomer complex beta-COP + H2O
?
show the reaction diagram
-
-
-
-
?
beta-transducin repeat containing protein + H2O
?
show the reaction diagram
-
-
-
-
?
beta2-adaptin + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
?
Boc-Leu-Met-7-amino-4-chloromethylcoumarin
?
show the reaction diagram
-
-
-
-
?
Boc-Val-Leu-Lys-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
caspase-3 + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
collapsin response mediator protein-1 + H2O
?
show the reaction diagram
-
collapsin response mediator protein-1 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-2 + H2O
?
show the reaction diagram
-
collapsin response mediator protein-2 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-4 + H2O
?
show the reaction diagram
-
collapsin response mediator protein-4 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-5 + H2O
?
show the reaction diagram
-
-
-
-
?
cortactin + H2O
?
show the reaction diagram
-
-
-
-
?
crystallin + H2O
?
show the reaction diagram
cyclin dependent kinase-5 + H2O
p25-CDK5
show the reaction diagram
-
-
-
-
?
dihydropteridine reductase + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
cleavage of the 6Arg-7Arg bond
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
filamin A + H2O
?
show the reaction diagram
-
-
-
-
?
focal adhesion kinase + H2O
?
show the reaction diagram
-
the preferred calpain cleavage site is between the two C-terminal proline-rich regions after Ser-745
-
-
?
frequenin homolog + H2O
?
show the reaction diagram
-
-
-
-
?
FRET-based substrate PLFAER + H2O
?
show the reaction diagram
-
10 microM, pH 7.4, 1 mM of CaCl2 added to initiate the reaction
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
show the reaction diagram
heterogeneous nuclear ribonucleoprotein F + H2O
?
show the reaction diagram
-
-
-
-
?
heterogeneous nuclear ribonucleoprotein K + H2O
?
show the reaction diagram
-
-
-
-
?
IkappaBalpha + H2O
?
show the reaction diagram
internexin + H2O
?
show the reaction diagram
-
-
-
-
?
IP3R1 + H2O
?
show the reaction diagram
-
in presence of Ca2, m-calpain cleaves IP3R1 in the endoplasmic lumen
-
-
?
laminin receptor 1 + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-enkephalin + H2O
?
show the reaction diagram
-
cleaved only slightly at the 1Tyr-2Gly bond
-
-
?
mammalian actin-binding protein-1 + H2O
?
show the reaction diagram
-
the preferred cleavage site occurs between the actin-binding domain and the proline-rich region, generating a C-terminal mAbp1 fragment
-
-
?
Met-enkephalin + H2O
?
show the reaction diagram
-
cleaved only slightly at the 1Tyr-2Gly bond
-
-
?
microtubule-associated protein 1
?
show the reaction diagram
-
-
-
-
?
microtubule-associated protein 1B + H2O
?
show the reaction diagram
-
-
-
-
?
microtubule-associated protein 2
?
show the reaction diagram
-
-
-
-
?
myocillin + H2O
?
show the reaction diagram
myosin II heavy chain + H2O
?
show the reaction diagram
-
rapid proteolysis
-
-
?
N-acetyl-LLY-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-LLY + 7-amino-4-trifluoromethylcoumarin
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
-
-
-
-
?
Na+/Ca2+ exchanger + H2O
82000 Da fragment + ?
show the reaction diagram
-
-
-
-
?
Na+/Ca2+ exchanger-1 + H2O
82 kDa fragment + ?
show the reaction diagram
-
calcium-dependent proteolytic cleavage of Na+/Ca2+ exchanger-1 occurs in the caveolae vesicles
-
-
?
NCX1 + H2O
?
show the reaction diagram
-
-
-
-
?
neurofilament + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
cleavage of the 3Tyr-4Glu bond and the 5Asn-6Lys bond
-
-
?
nucleolin + H2O
?
show the reaction diagram
-
-
-
-
?
p35 + H2O
25000 Da fragment of p35 + ?
show the reaction diagram
-
calpain-specific substrate
-
-
?
proteolysis-resistant fragment 130 + H2O
proteolysis-resistant fragment 45 + ?
show the reaction diagram
-
-
-
-
?
proteolysis-resistant fragment 72 + H2O
proteolysis-resistant fragment 45 + ?
show the reaction diagram
-
-
-
-
?
RRRRRRRR-(EDANS)-GQQEVYGMMPRDG-(DABCYL) + H2O
?
show the reaction diagram
-
-
-
-
?
selenoprotein K + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
succinyl-bovine-serum-albumin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-casein + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-insulin B + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
succinyl-Leu-Met-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Met + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
succinyl-protamine + H2O
?
show the reaction diagram
-
-
-
-
?
synaptotagmin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
t-Boc-Leu-Met-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
talin + H2O
?
show the reaction diagram
tert-butoxycarbonyl-Leu-Met-7-amido-4-chloromethylcoumarin + H2O
tert-butoxycarbonyl-Leu-Met + 7-amino-4-chloromethylcoumarin
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
-
-
-
-
?
TPLKSPPPSPR + H2O
?
show the reaction diagram
-
efficient substrate
-
-
?
transgelin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
ubiquitin-activating enzyme E1 + H2O
?
show the reaction diagram
-
-
-
-
?
upstream stimulatory factor + H2O
?
show the reaction diagram
-
-
-
-
?
vimentin + H2O
?
show the reaction diagram
-
-
-
-
?
voltage dependent anion channel + H2O
?
show the reaction diagram
-
-
-
-
?
voltage-dependent anion channel + H2O
?
show the reaction diagram
-
mitochondrial m-calpain truncates voltage-dependent anion channel in Ca2+-dependent manner
-
-
?
desmin + H2O
additional information
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-2 spectrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-spectrin + H2O
145000 Da fragment + ?
show the reaction diagram
-
-
-
-
?
aminopeptidase B + H2O
?
show the reaction diagram
-
-
-
-
?
androgen receptor + H2O
?
show the reaction diagram
-
-
-
-
?
beta-transducin repeat containing protein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
caspase-3 + H2O
?
show the reaction diagram
-
-
-
-
?
collapsin response mediator protein-1 + H2O
?
show the reaction diagram
-
collapsin response mediator protein-1 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-2 + H2O
?
show the reaction diagram
-
collapsin response mediator protein-2 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-4 + H2O
?
show the reaction diagram
-
collapsin response mediator protein-4 is cleaved by calpain-2 at the C-terminus
-
-
?
collapsin response mediator protein-5 + H2O
?
show the reaction diagram
-
-
-
-
?
cortactin + H2O
?
show the reaction diagram
-
-
-
-
?
crystallin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
frequenin homolog + H2O
?
show the reaction diagram
-
-
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
show the reaction diagram
-
GAP-43 cleavage at Ser41 residue in synaptosomes is mediated by m-calpain
-
-
?
heterogeneous nuclear ribonucleoprotein F + H2O
?
show the reaction diagram
-
-
-
-
?
heterogeneous nuclear ribonucleoprotein K + H2O
?
show the reaction diagram
-
-
-
-
?
IkappaBalpha + H2O
?
show the reaction diagram
-
a parallel pathway that degrades IkappaBalpha and activates NF-kappaB activation independently of the ubiquitin-proteasome pathway
-
-
?
internexin + H2O
?
show the reaction diagram
-
-
-
-
?
IP3R1 + H2O
?
show the reaction diagram
-
in presence of Ca2, m-calpain cleaves IP3R1 in the endoplasmic lumen
-
-
?
laminin receptor 1 + H2O
?
show the reaction diagram
-
-
-
-
?
mammalian actin-binding protein-1 + H2O
?
show the reaction diagram
-
the preferred cleavage site occurs between the actin-binding domain and the proline-rich region, generating a C-terminal mAbp1 fragment
-
-
?
microtubule-associated protein 1B + H2O
?
show the reaction diagram
-
-
-
-
?
myocillin + H2O
?
show the reaction diagram
-
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
-
-
?
NCX1 + H2O
?
show the reaction diagram
-
-
-
-
?
neurofilament + H2O
?
show the reaction diagram
-
-
-
-
?
nucleolin + H2O
?
show the reaction diagram
-
-
-
-
?
p35 + H2O
25000 Da fragment of p35 + ?
show the reaction diagram
-
calpain-specific substrate
-
-
?
selenoprotein K + H2O
?
show the reaction diagram
-
cleavage occurs only in unactivated macrophages, m-calpain cleavage at Arg81-Gly82 generates the two selenoprotein K isoforms
-
-
?
synaptotagmin-1 + H2O
?
show the reaction diagram
-
-
-
-
?
transgelin-3 + H2O
?
show the reaction diagram
-
-
-
-
?
ubiquitin-activating enzyme E1 + H2O
?
show the reaction diagram
-
-
-
-
?
vimentin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
-
millimolar concentrations of Al3+ activate at at submillimolar concentrations of Ca2+
Co2+
-
5 mM, activates
Cu2+
-
activates
K+
-
5 mM, activates in presence of 5 mM Ca2+
Na+
-
5 mM, activates in presence of 5 mM Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
70 kDa calpastatin
-
-
-
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
acetyl-Leu-Leu-Nle-CHO
Al3+
-
inactivation at millimolar concentration of Ca2+
ALLN
-
-
alpha2-Macroglobulin
-
0.05 mg/ml, 11% inhibition
-
antipain
benzyloxycarbonyl-L-leucyl-L-leucinal
-
-
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
calpain inhibitor I
calpain inhibitor II
calpastatin
calpastatin II
-
-
-
Calpeptin
caplastatin 2
-
-
-
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
-
-
GAP-43-3
indomethacin
-
-
iodoacetamide
-
1 mM, 64% inhibition
iodoacetic acid
Leupeptin
MDL-28170
-
-
MDL28170
Mg2+
-
5 mM, inhibits in presence of 5 mM Ca2+
Mn2+
-
2.5 mM, strong
N-acetyl-L-leucyl-L-leucyl-L-methioninal
-
-
N-acetyl-Leu-Leu-Met
-
-
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
NS-398
-
-
PD150606
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
-
SC-560
-
-
SNJ-1945
-
-
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
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
calcium lactate
-
-
dithiothreitol
glutathione
TNF-alpha
-
activates cytosolic enzyme
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.5
Boc-Val-Leu-Lys-methylcoumarin
-
pH 7.5, room temperature
2.2
succinyl-bovine-serum albumin
-
pH 7.5, 25C
-
10
succinyl-casein
-
pH 7.5, 25C
-
453.7
succinyl-insulin B
-
pH 7.5, 25C
-
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 - 2.13
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
3.18
succinyl-Leu-Tyr-methylcoumarin
-
pH 7.5, room temperature
101.3
succinyl-protamine
-
pH 7.5, 25C
-
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.341
Boc-Val-Leu-Lys-methylcoumarin
Struthio camelus
-
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
Struthio camelus
-
pH 7.5, room temperature
0.186 - 0.189
succinyl-Leu-Met-7-amido-4-methylcoumarin
0.083 - 0.084
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
0.04
succinyl-Leu-Tyr-methylcoumarin
Struthio camelus
-
pH 7.5, room temperature
0.546
t-Boc-Leu-Met-methylcoumarin
Struthio camelus
-
-
1.06 - 1.08
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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 22C
-
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 22C
-
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 22C
-
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 22C
-
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 22C
-
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 22C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00014
(2S)-3-phenyl-2-([[(2S)-1-(phenylsulfonyl)pyrrolidin-2-yl]carbonyl]amino)propanoic acid
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00041
(2S)-4-methyl-2-[(phenylsulfonyl)amino]pentanoic acid
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00000052
110 kDa calpastatin
Bos taurus
-
in 100 mM imidazole-HCl buffer (pH 7.5),5 mM cysteine and 5 mM CaCl2, at 30C
-
0.0000008
70 kDa calpastatin
Bos taurus
-
in 100 mM imidazole-HCl buffer (pH 7.5),5 mM cysteine and 5 mM CaCl2, at 30C
-
0.00024
ethyl N-(phenylsulfonyl)-L-leucyl-L-phenylalaninate
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00015
MDL28170
Rattus norvegicus
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
1 mM CaCL2 added to start reaction
7.5
-
-
7.5 - 8
7.7
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
-
pH 5.0: about 50% of maximal activity, pH 8.5: about 30% of maximal activity
6 - 8
-
pH 6.0: about 40% of maximal activity, pH 8.0: about 50% of maximal activity, enzyme from retina and brain
6 - 8.5
-
pH 6.0: about 50% of maximal activity, pH 8.5: about 60% of maximal activity
6.5 - 7.5
-
activity of m-calpain is greater at pH 7.5 than at pH 6.5
6.5 - 8.5
-
pH 6.5: about 50% of maximal activity, pH 8.5: about 40% of maximal activity
additional information
-
the enzyme is not proteolytically active at pH 5.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
-
10C: about 60% of maximal activity, 40C: about 45% of maximal activity
10 - 45
-
10C: about 60% of maximal activity, 45C: about 35% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
calpain 2 is important for both the formation of invadopodia and invasive capacity of breast cancer cells
Manually annotated by BRENDA team
-
nCL-2 is localized strictly to the surface cells in the gastric epithelium and the mucus-secreting goblet cells in the duodenum
Manually annotated by BRENDA team
-
analysis from E8.5 to 14.5 stages indicates high levels of capn2 expression in the nervous system, heart and mesodermal tissues. Up-regulation is maintained during later developmental stages in proliferating cells and in precursor cells involved in muscle (myoblasts) or bone formation (chondrocytes). At later developmental stages, elevated mRNA levels coincide with CAPN2 nuclear localization in these cell types, while differentiated cells maintain cytoplasmic expression
Manually annotated by BRENDA team
-
pulmonary microvascular endothelial cell. Incubation of the cells with vascular endothelial growth factor results in dose- and time-dependent increases in calpain activity and protein content of calpain-2. Vascular endothelial growth factor does not change the protein contents of calpain-1 and the small subunit or of calpastatin. Inhibition of calpain activity by siRNA directed against calpain-2 and by overexpression of calpastatin prevents vascular endothelial growth factor-induced increases in actin stress fibers in endothelial cells and angiogenesis
Manually annotated by BRENDA team
-
calpain 2 is first expressed late in embryonic development and localizes to the lens epithelium and transition zone
Manually annotated by BRENDA team
-
nCL-2 is localized strictly to the surface cells in the gastric epithelium and the mucus-secreting goblet cells in the duodenum
Manually annotated by BRENDA team
-
calpain 2 localizes to GM-3-rich lipid rafts at the leading edge
Manually annotated by BRENDA team
-
prefominantly localized in the growing hyphal and rhizoidal apices
Manually annotated by BRENDA team
-
membrane abnormalities and altered signaling pathways observed in Duchenne muscular dystrophy lymphocytes may be due to the increased association of calpain II onto membrane and cytosol
Manually annotated by BRENDA team
-
fibro-cartilagenous disks from meniscal tissue explants
Manually annotated by BRENDA team
-
primary neutrophil
Manually annotated by BRENDA team
-
outer segment
Manually annotated by BRENDA team
-
originated from kidney
Manually annotated by BRENDA team
-
calpain 2 activity is critical for the life cycle of echovirus 1 and important in the multiplication of the viral RNA genome
Manually annotated by BRENDA team
-
active calpain 2 is concentrated in the trailing edge of the migrating T cell
Manually annotated by BRENDA team
-
physiological shear stress elicits Ca2+ influx-sensitive activation of m-calain in umbilical vein endothelial cells
Manually annotated by BRENDA team
-
present in very low amounts, only 0.0033%
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
3.9% of the activity
-
Manually annotated by BRENDA team
-
in caveolae vesicles isolated from bovine pulmonary artery smooth muscle plasma membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
-
active form, SDS-PAGE
70000
-
SDS-PAGE
79920
-
m-calpain large subunit, calculated from amino acid sequence
90000
-
gel filtration
100000
-
-
105000
-
gel filtration
110000
115000
-
gel filtration
124000
-
gel filtration
160000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
side-chain modification
-
calpain-2 is small ubiquitin-like modifier-modified at lysine residue 390, sumoylation is important for calpain-2 activity
additional information
-
the enzyme is neither glycosylated nor phosphorylated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
full-length human m-calpain containing an N-terminal Gly-Arg-Arg-Asp-Arg-Ser L-chain elongation overexpressed in a baculovirus expression system. Crystals grown by vapor diffusion. The 2.3 A crystal structure of full length heterodimeric m-calpain crystallized in the absence of calcium reveals an oval disc-like shape, with the papain-like catalytic domain dII and the two calmodulin, like domains dIV+dVI occupying opposite poles, and the tumor necrosis factor alpha-like beta-sandwich domain dIII and the N-terminal segments dI+dV located between
-
2.6 A crystal structure of m-calpain that has a C-terminal histidine-tag and a mutation of the active site C105S in the large subunit in the Ca2+-free form
-
calpastatin inhibitory domain 1 crystallized with calpain 2, calpastatin inhibitory domain 4 crystallized with calpain 2
-
crystallization of recombinant C105S mutant enzyme by hanging drop method
-
the refined crystal structure of the mutant enzymes K226S, K230E, K234S and E504S in absence of Ca2+ are indistinguishable from wilde-type calpain; wild-type and mutant calpains
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
25C, 30 min, stable in presence of 20 mM 2-mercaptoethanol
644031
5.5
-
25C, 30 min, about 30% loss of activity
644031
6.5 - 7.5
-
25C, 30 min, stable in presence of 6 mM 2-mercaptoethanol
644031
8.5
-
25C, 30 min, about 50% loss of activity
644031
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48.5
-
10 min, 50% loss of activity
54
-
pH 7.5, 10 min, 50% loss of activity
55
-
10 min, in absence of Ca2+, about 10% loss of activity
58
-
10 min, complete inactivation
61
-
10 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
50% inactivation by autolysis after 1 min at 30C, pH 7.5, 10 mM Ca2+
-
50% inhibition by trypsin after 3 min at 30C, pH 7.5
-
bovine fetuin A stabilizes proteolytic activity of purified m-calpain incubated in the presence of mM calcium chloride and prevents calcium-dependent m-calpain aggregation
-
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
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the pre-incubation of m-calpain with H2O2 results in a significant decrease of m-calpain activity under non-reducing condition. The addition of calcium lactate (5 mM) to the pre-incubation mixture of m-calpain with H2O2 (0.05 mM) results in a more extensive loss of m-calpain activity compared to the equal amount of CaCl2 addition to the pre-incubation mixture
-
717628
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for 8 days, 70% inactivation after 2 months
-
-20C, stable for 8 days, complete inactivation after 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-cellulose column chromatography, phenyl-Sepharose column chromatography, DEAE-TSK column chromatography, and Reactive Red gel filtration
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, phenyl-Sepharose column chromatography, Reactive Red column chromatography, and DEAE-TSK anion exchange column chromatography
-
DEAE Sephacel gel filtration
-
DEAE-Sepharose CL-6B column chromatography
-
DEAE-Sepharose column chromatography
-
E-F hand structure-domains
-
HisTrap column chromatography
-
large-scale
-
m-calpain
-
recombinant enzyme
recombinant wild-type and mutant enzymes; wild-type and mutant calpains
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 629 bp fragment is cloned into the EcoRV site of pBluescript II KS+ vector
-
cDNA fragments corresponding to the domains with E-F hand structures in the large and small subunits are inserted into an expression vector pIC18 or pUC8. The resulting plasmids are used to transform Escherichia coli and isopropyl-1-thio-beta-D-galactoside-inducible expression is induced
-
cloning of the cDNA for the large subunit
-
coexpression from large-subunit and small-subunit plasmids in Escherichia coli strain BL21(DE3)
-
development of an adenoviral vector harboring calpain-2 siRNA expression unit in which sense and anti-sense strands composing the siRNA duplex are connected by a loop and transcribed into a siRNA in porcine pulmonary artery endothelial cells. The adenoviral vector harboring calpain-2 siRNA expression unit is a valuable tool to study the biology of calpains
-
expressed in Escherichia coli
-
expression of mutated calpain 2 C105A is driven in lens by coupling the mutated gene to the betaB1-crystallin promoter
-
functional analysis of the upstream region of the gene for the large subunit by means of transient expression assay on HeLa cells using chloramphenicol transferase constructs identifies four negative regulatory regions tandemly reiterated just upstream of the promoter region, P1 and P2
-
isolation of cDNA clone for the 80000 Da subunit
-
m-calpain is produced in a soluble form using a baculovirus expression system
-
molecular cloning of the cDNA for the 80000 Da subunit and expression in Escherichia coli
-
the bacterial production of recombinant rat calpain II is improved greatly by the use of two compatible plasmids for the two subunits. The calpain small subunit C-terminal fragment is expressed from a new A15-based vector created by cloning T7 contol elements into pACYC177. This vector is compatible with the ColE1-based pET-24d(+) vector containing the calpain large subunit and the yield of calpain activity is increased at least 16fold by coexpression from theses two vectors. A high level of activity is also obtained from a bicistronic construct containing the subunit cDNAs under the control of one T7 promoter
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
0.1 mM indomethacin and 0.1 mM NS-398 decrease expression of calpain 2 in total membrane fractions and in plasma membranes by 70%, while 0.001 mM SC-560 decreases expression of calpain 2 in total membrane fractions and in plasma membranes by 30%
-
a 6-day treatment with siRNA results in an about 60% reduction of calpain 2 protein levels in R1 cells
-
a heat stress stimulus induces massive germ cells apoptosis, which is associated with an increase in the levels of mRNA encoding calpain 2
-
brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation
-
calpain 2 expression levels increase throughout stem cell differentiation
-
calpain 2 is upregulated in mouse pancreas exposed to caerulein for 12 h
-
calpain activation occurs during reperfusion, but only after intracellular pH normalization, and is not prevented by inhibiting its translocation during ischemia with methyl-beta-cyclodextrin; m-calpain activation occurs during reperfusion, but only after intracellular pH normalization, and is not prevented by inhibiting its translocation during ischemia with methyl-beta-cyclodextrin
-
endoplasmic reticulum stress stimulates calpain II activation, interleukin-13 enhances endoplasmic reticulum stress-regulated calpain activation and calpain-II expression in lipopolysaccaride-activated microglia
-
incubation of human retinal microvascular endothelial cells with vascular endothelial growth factor results in 1.6fold increased activity of calpain 2 at 24 h
-
inhibition of MEK1/2 using PD98059 reduces the expression of calpain-2
-
m-calpain expression levels in aorta in siRNAtreated mice are significantly diminished by 63.5% in comparison to those in control RNA-transfected mice with no alteration of m-calpain or beta-actin expression
-
p38 MAPK and JNK are required to stimulate m-calpain activity when TRPM7 is overexpressed, TRPM7-mediated activation of m-calpain is not dependent on the nature of the divalent conducted by the channel
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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; mutation decreases specific activity to 90% compared to wild-type enzyme
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
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; 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; mutation has no significant effect on specific activity
K234E
-
mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme
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; mutation decreases specific activity to 81% compared to 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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine