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Information on EC 3.4.22.53 - calpain-2 and Organism(s) Sus scrofa and UniProt Accession P43367

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.53 calpain-2
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This record set is specific for:
Sus scrofa
UNIPROT: P43367 not found.
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The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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broad endopeptidase specificity
Synonyms
m-calpain, calpain ii, calpain-2, calpain 2, calpain2, ncl-2, milli-calpain, mitochondrial m-calpain, calcium-activated neutral protease ii, calpain-2-like, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cal II
-
-
calcium-activated neutral protease II
-
-
-
-
calpain 2
-
-
-
-
calpain II
calpain xCL-2 (Xenopus leavis)
-
-
-
-
CAPN2 g.p. (Homo sapiens)
-
-
-
-
m-calpain
milli-calpain
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
702693-80-9
-
78990-62-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
MARCKS protein + H2O
?
show the reaction diagram
casein + H2O
?
show the reaction diagram
-
-
-
-
?
GAP-43 + H2O
GAP-43-3 + ?
show the reaction diagram
-
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
-
-
?
microtubule-associated protein 1
?
show the reaction diagram
-
-
-
-
?
microtubule-associated protein 2
?
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
-
-
?
succinyl-Leu-Leu-Val-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
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
MARCKS protein + H2O
?
show the reaction diagram
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
-
-
?
casein + 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
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
calpastatin
-
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
-
-
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
-
NaCl
-
m-calpain is more active at 165 mM NaCl than at 295 mM NaCl
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
calcium lactate
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
m-calpain
7.7
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAN2_PIG
324
0
37809
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
1 * 80000 + 1 * 29000, SDS-PAGE
80000
-
1 * 80000 + 1 * 29000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
1 * 80000 + 1 * 29000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54
-
pH 7.5, 10 min, 50% loss of activity
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
large-scale
-
m-calpain
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 629 bp fragment is cloned into the EcoRV site of pBluescript II KS+ vector
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sun, W.; Ji, S.Q.; Ebert, P.J.; Bidwell, C.A.; Hancock, D.L.
Cloning the partial cDNAs of mu-calpain and m-calpain from porcine skeletal muscle
Biochimie
75
931-936
1993
Sus scrofa (P43367), Sus scrofa
Manually annotated by BRENDA team
Fukui, I.; Toyohara, H.; Ito, K.; Hamakubo, T.; Murachi, T.
Molecular and catalytic characterization of intact heterodimeric and derived monomeric calpains isolated under different conditions from pig polymorphonuclear leukocytes
Biochemistry
27
3260-3267
1988
Sus scrofa
Manually annotated by BRENDA team
Yoshimura, N.; Tsukahara, I.; Murachi, T.
Calpain and calpastatin in porcine retina
Biochem. J.
223
47-51
1984
Sus scrofa
Manually annotated by BRENDA team
Kitahara, A.; Sasaki, T.; Kikuchi, T.; Yumoto, N.; Yoshimura, N.; Hatanaka, M.; Murachi, T.
Large-scale purification of porcine calpain I and calpain II and comparison of proteolytic fragments of their subunits
J. Biochem.
95
1759-1766
1984
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Zhang J.L.; Patel J.M.; Block E.R.
Hypoxia-specific upregulation of calpain activity and gene expression in pulmonary artery endothelial cells
Am. J. Physiol.
275
L461-L468
1998
Sus scrofa (P43367)
Manually annotated by BRENDA team
Maddock, K.R.; Huff-Lonergan, E.; Rowe, L.J.; Lonergan, S.M.
Effect of pH and ionic strength on mu- and m-calpain inhibition by calpastatin
J. Anim. Sci.
83
1370-1376
2005
Sus scrofa
Manually annotated by BRENDA team
Carlin, K.R.; Huff-Lonergan, E.; Rowe, L.J.; Lonergan, S.M.
Effect of oxidation, pH, and ionic strength on calpastatin inhibition of mu- and m-calpain
J. Anim. Sci.
84
925-937
2006
Sus scrofa
Manually annotated by BRENDA team
Zakharov, V.V.; Mosevitsky, M.I.
M-calpain-mediated cleavage of GAP-43 near Ser41 is negatively regulated by protein kinase C, calmodulin and calpain-inhibiting fragment GAP-43-3
J. Neurochem.
101
1539-1551
2007
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Kim, Y.; Huff-Lonergan, E.; Lonergan, S.
Effect of calcium lactate on m-calpain activity and protein degradation under oxidising conditions
Food Chem.
131
73-78
2012
Sus scrofa
-
Manually annotated by BRENDA team
Huang, Z.; Hoffmann, F.W.; Norton, R.L.; Hashimoto, A.C.; Hoffmann, P.R.
Selenoprotein K is a novel target of m-calpain, and cleavage is regulated by Toll-like receptor-induced calpastatin in macrophages
J. Biol. Chem.
286
34830-34838
2011
Sus scrofa
Manually annotated by BRENDA team
Ovat, A.; Li, Z.; Hampton, C.; Asress, S.; Fernandez, F.; Glass, J.; Powers, J.
Peptidyl alpha-ketoamides with nucleobases, methylpiperazine, and dimethylaminoalkyl substituents as calpain inhibitors
J. Med. Chem.
53
6326-6336
2010
Sus scrofa
Manually annotated by BRENDA team
Montgomery, D.S.; Yu, L.; Ghazi, Z.M.; Thai, T.L.; Al-Khalili, O.; Ma, H.P.; Eaton, D.C.; Alli, A.A.
ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins
Am. J. Physiol. Cell Physiol.
313
C42-C53
2017
Sus scrofa (P43367)
Manually annotated by BRENDA team