Information on EC 3.4.22.B30 - calpain 10

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.B30
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
calpain 10
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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
78990-62-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
strain 129/SvJ
SwissProt
Manually annotated by BRENDA team
strain NOD
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP synthase beta + H2O
?
show the reaction diagram
FITC-casein + H2O
FITC + casein
show the reaction diagram
ND6 subunit of complex I + H2O
?
show the reaction diagram
NDUFB8 + H2O
?
show the reaction diagram
NDUFV2 + H2O
?
show the reaction diagram
peptide + H2O
hydrolyzed peptide
show the reaction diagram
SLLVY-7-amido-4-methylcoumarin + H2O
SLLVY + 7-amino-4-methylcoumarin
show the reaction diagram
SLLVYAMC + H2O
SLLVY + AMC
show the reaction diagram
SNAP-25 + H2O
?
show the reaction diagram
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
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-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
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
ATP synthase beta + H2O
?
show the reaction diagram
NDUFB8 + H2O
?
show the reaction diagram
peptide + H2O
hydrolyzed peptide
show the reaction diagram
SNAP-25 + H2O
?
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
calpastatin
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Calpeptin
CYGAK
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inhibitory activity of CYGAK to calpain 10 is independent of Ca2+
CYGAK disulfide
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valuable tool to prevent Ca2+ induced mitochondrial dysfunction and explore the function of calpain 10
N-[(2R)-4-hydroxy-1-oxobutan-2-yl]-N2-(phenylcarbamothioyl)-L-leucinamide
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binding structure, the inhibitor shows interactions with the Cys115, Gly207, Gly20,8 and Gly271 residues, overview. Reversible intramolecular conversion of the cyclic hemiacetal form of SNJ-1715 to the free aldehyde form
N-[(3R)-2-hydroxytetrahydrofuran-3-yl]-N2-(phenylcarbamothioyl)-L-leucinamide
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binding structure, the inhibitor shows interactions with the Cys115, Gly207, Gly20,8 and Gly271 residues, overview. Reversible intramolecular conversion of the cyclic hemiacetal form of SNJ-1715 to the free aldehyde form
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
angiotensin II
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activates the enzyme in vivo, reduced by pan-calpain inhibitors
glucose
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gradual increase after 3.5 days of exposure
intralipid
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fat emulsion consisting of 12% palmitic acid, 4% stearic acid, 21% oleic acid, 53% linoleic acid, 7% alpha-linoleic acid, and 3% other acids, after 24 h exposure, increase in CAPN10 mRNA in response to insulin in subjects with normal glucose tolerance
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
CYGAK
Rattus norvegicus
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0.24
CYGRK
Rattus norvegicus
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0.29
CYGRKK
Rattus norvegicus
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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two major isoforms with intact N-terminus but different C-terminal T domains
Manually annotated by BRENDA team
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it is proposed that a defective CAPN10 pre-mRNA processing is responsible for the decreased levels of SNP-43 A-allele transcripts in peripheral white cells of healthy and T2D individuals
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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cultured alphaTN4-1 lens epithelial cells
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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x * 50000, diverse isoforms of calpain-10 are produced by alternative splicing. The isoform that shows the highest levels of expression is the one of approximately 50000 Da
64000
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in the cytosol, SDS-PAGE
74527
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x * 74527, calculation from nucleotide sequence
additional information
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immuno-stained bands at 26000, 54000 and 72000 Da between cytosol and membranes, SDS-PAGE, the 54000 Da isoform is associated with a synaptosomal-associated protein of 25000 Da
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in INS-1 cells
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expression in the baculovirus system
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genotyping and association with type 2 diabetes mellitus , detailed overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
calpain-10 expression is elevated by 64% in pancreatic islets from patients with type 2 diabetes compared with non-diabetic donors
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calpain-10 is overexpressed and activated through the inhibition of ryanodine receptor 2 under hypoglycemic and high fatty acid conditions, causing caspase-3-independent beta-cell death
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chronic high glucose down-regulates mitochondrial calpain 10. High glucose (17 mM) decreases mitochondrial calpain 10 mRNA and protein at 96 h compared with cells incubated with 0 or 5 mM glucose or 17 mM D-mannitol. Renal calpain 10 protein and mRNA are specifically decreased in streptozotocin-induced diabetic rats with kidney dysfunction
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mitochondrial calpain activity does not change with 5mM glucose or 17 mM D-mannitol
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renal calpain 10 protein and mRNA are specifically decreased in ob/ob diabetic mice
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
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the development of inhibitors against calpain-10 may be useful as therapeutic agents for a number of calpainopathies
medicine