Information on EC 3.4.22.B37 - calpain B

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.B37
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
calpain B
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
broad endopeptidase specificity
show the reaction diagram
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-
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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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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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calpainB is required for acute myeloid leukemia 1-ETO-induced blood cell disorders in Drosophila
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
calpain B + H2O
?
show the reaction diagram
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initial autolysis of calpain B seems to occur intramolecularly
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?
casein + H2O
?
show the reaction diagram
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?
microtubule-associated protein 2c + H2O
?
show the reaction diagram
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-
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?
N-succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-L-Leu-L-Tyr + 7-amino-4-methyl-coumarin
show the reaction diagram
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-
-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methyl-coumarin + H2O
?
show the reaction diagram
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pH 7.5
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-
?
peptide + H2O
hydrolyzed peptide
show the reaction diagram
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?
additional information
?
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N-terminal autolysis in a Ca2+-dependent manner which runs parallel with the enzyme activation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
carbobenzoxy-valinyl-phenylalaninal
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N-acetyl-leucyl-leucyl-norleucinal
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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high activity
Manually annotated by BRENDA team
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in the late embryos high activity is detected in the tracheas and their orifices as well as in the larynx
Manually annotated by BRENDA team
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in the early larval stage the calpain B level is very low. After this stage the level rises strongly, indicating the vigorous transcription of the CalpB gene up to the third larval stage, then the level becomes constant in the pupa and imago
Manually annotated by BRENDA team
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in the late embryos high activity is detected in the tracheas and their orifices as well as in the larynx
Manually annotated by BRENDA team
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activity is strongly detectable in follicular and border cells of the oocyte
Manually annotated by BRENDA team
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high expression
Manually annotated by BRENDA team
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in the late embryos high activity is detected in the tracheas and their orifices as well as in the larynx
Manually annotated by BRENDA team
additional information
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calpain B is detectable in all developmental stages of the fly
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
81000
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estimated from amino acid sequence, activated enzyme after N-terminal autolysis
83000
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1 * 83000, SDS-PAGE
88900
estimated from amino acid sequence
90134
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x * 90134, calculation from nucleotide sequence
104000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
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phosphorylation elevates the Ca2+ sensitivity of the protease. The activation of the extracellular signal-regulated protein kinase pathway by extracellular signals results in the phosphorylation and activation of calpain B in fruit flies
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA encoding for domain III is expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
mutant enzyme Q73G/N74V/A75P/N223A/Q224V expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BIII-D613N/D614N
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retains 30% of the wild-type Ca2+-binding capacity
BIII-D617N/D618
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retains 60% of the wild-type Ca2+-binding capacity
BIII-E610A/D611A/P612A, delta613-620 deletion mutant
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unable to bind Ca2+
BIII-E610Q/D611N/D613N/D614N
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retains 16.2% of the wild-type Ca2+-binding capacity
BIII-E615Q/D616N/D617N/D618N
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retains 36% of the wild-type Ca2+-binding capacity
BIII-P612A, delta613-620 deletion mutant
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retains one-third of the original Ca2+- binding capacity
C314A
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inactive
D613N/D614N
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enhances specific activity to 114% of the wild-type activity
D617N/D618N
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reduces specific activity to 66% of the wild-type activity
Q73G/N74V/A75P/N223A/Q224V
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mutation within the autolytic cleavage sites, autolysis is not arrested by the mutations but its site shifts to new, nearby peptide bonds. In the case of site between Q224 and N225, two new sites emerge: one at F215-T216 and one at G230-R231. In the case of site between N74 and A75, modification gives rise to low intensity, blurred bands which can not be analyzed by sequencing
S845E
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the mutation causes a small but reproducible increase in the activation of calpain B
T747E
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the mutation causes a large increase in the activation of calpain B
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
removal of urea by stepwise dialysis in buffer A (50 mM Tris, pH 7.5, 150 mM NaCl) containing 1 M NaCl and 8-4-2-1-0.5-0 M urea, at least for 8 hours in each case
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