Information on EC 3.4.22.53 - calpain-2

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.53
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RECOMMENDED NAME
GeneOntology No.
calpain-2
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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
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endopeptidase; peptides, endopeptidase
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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
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
quail
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
Tilapia nilotica * Tilapia aurea
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Manually annotated by BRENDA team
trout
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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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
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-
-
-
?
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
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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
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-
?
beta-neoendorphin + H2O
?
show the reaction diagram
-
cleavage of the 6Arg-7Lys bond
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-
?
beta-subunit of coatomer complex beta-COP + H2O
?
show the reaction diagram
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-
-
-
?
beta-transducin repeat containing protein + H2O
?
show the reaction diagram
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-
-
-
?
beta2-adaptin + H2O
?
show the reaction diagram
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-
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?
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
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-
?
Boc-Leu-Met-7-amino-4-chloromethylcoumarin
?
show the reaction diagram
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-
-
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?
Boc-Val-Leu-Lys-methylcoumarin + H2O
?
show the reaction diagram
-
-
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?
casein + H2O
?
show the reaction diagram
caspase-3 + H2O
?
show the reaction diagram
-
-
-
-
?
collapsin response mediator protein 1 + H2O
?
show the reaction diagram
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-
-
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?
collapsin response mediator protein 2 + H2O
?
show the reaction diagram
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-
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?
collapsin response mediator protein 3 + H2O
?
show the reaction diagram
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?
collapsin response mediator protein 4 + H2O
?
show the reaction diagram
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?
collapsin response mediator protein-1 + H2O
?
show the reaction diagram
-
collapsin response mediator protein-1 is cleaved by calpain-2 at the C-terminus
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-
?
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
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collapsin response mediator protein-4 is cleaved by calpain-2 at the C-terminus
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?
collapsin response mediator protein-5 + H2O
?
show the reaction diagram
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-
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?
cortactin + H2O
?
show the reaction diagram
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?
crystallin + H2O
?
show the reaction diagram
cyclin dependent kinase-5 + H2O
p25-CDK5
show the reaction diagram
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?
dihydropteridine reductase + H2O
?
show the reaction diagram
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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
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?
dynorphin (1-13) + H2O
?
show the reaction diagram
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cleavage of the 6Arg-7Arg bond
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?
Fibronectin + H2O
?
show the reaction diagram
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?
filamin A + H2O
?
show the reaction diagram
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?
focal adhesion kinase + H2O
?
show the reaction diagram
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the preferred calpain cleavage site is between the two C-terminal proline-rich regions after Ser-745
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?
frequenin homolog + H2O
?
show the reaction diagram
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?
FRET-based substrate PLFAER + H2O
?
show the reaction diagram
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10 microM, pH 7.4, 1 mM of CaCl2 added to initiate the reaction
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?
GAP-43 + H2O
GAP-43-3 + ?
show the reaction diagram
heterogeneous nuclear ribonucleoprotein F + H2O
?
show the reaction diagram
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?
heterogeneous nuclear ribonucleoprotein K + H2O
?
show the reaction diagram
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?
IkappaBalpha + H2O
?
show the reaction diagram
internexin + H2O
?
show the reaction diagram
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?
IP3R1 + H2O
?
show the reaction diagram
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in presence of Ca2, m-calpain cleaves IP3R1 in the endoplasmic lumen
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?
laminin receptor 1 + H2O
?
show the reaction diagram
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?
Leu-enkephalin + H2O
?
show the reaction diagram
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cleaved only slightly at the 1Tyr-2Gly bond
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?
mammalian actin-binding protein-1 + H2O
?
show the reaction diagram
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the preferred cleavage site occurs between the actin-binding domain and the proline-rich region, generating a C-terminal mAbp1 fragment
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?
Met-enkephalin + H2O
?
show the reaction diagram
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cleaved only slightly at the 1Tyr-2Gly bond
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?
microtubule-associated protein 1
?
show the reaction diagram
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?
microtubule-associated protein 1B + H2O
?
show the reaction diagram
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?
microtubule-associated protein 2
?
show the reaction diagram
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?
myocillin + H2O
?
show the reaction diagram
myosin II heavy chain + H2O
?
show the reaction diagram
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rapid proteolysis
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?
N-acetyl-LLY-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-LLY + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
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?
N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
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?
Na+/Ca2+ exchanger + H2O
82000 Da fragment + ?
show the reaction diagram
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?
Na+/Ca2+ exchanger-1 + H2O
82 kDa fragment + ?
show the reaction diagram
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calcium-dependent proteolytic cleavage of Na+/Ca2+ exchanger-1 occurs in the caveolae vesicles
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?
NCX1 + H2O
?
show the reaction diagram
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-
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?
neurofilament + H2O
?
show the reaction diagram
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-
-
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?
neurotensin + H2O
?
show the reaction diagram
-
cleavage of the 3Tyr-4Glu bond and the 5Asn-6Lys bond
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?
nucleolin + H2O
?
show the reaction diagram
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?
p35 + H2O
25000 Da fragment of p35 + ?
show the reaction diagram
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calpain-specific substrate
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?
proteolysis-resistant fragment 130 + H2O
proteolysis-resistant fragment 45 + ?
show the reaction diagram
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?
proteolysis-resistant fragment 72 + H2O
proteolysis-resistant fragment 45 + ?
show the reaction diagram
-
-
-
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?
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
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-
-
-
?
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
-
-
-
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?
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
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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+
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
4920
0.0399 - 0.0404
succinyl-Leu-Met-7-amido-4-methylcoumarin
13002
0.0394 - 0.0395
succinyl-Leu-Tyr-7-amido-4-methylcoumarin
11267
0.131 - 0.133
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
11332
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 - 8
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
-
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
-
-
Automatic Mining of ENzyme DAta
-
present in very low amounts, only 0.0033%
Manually annotated by BRENDA team