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Information on EC 3.4.22.B37 - calpain B and Organism(s) Drosophila melanogaster and UniProt Accession Q9VT65
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3.4.22.B37 calpain BSpecify your search results
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- 3.4.22.B37
- calpains
- drosophila
- melanogaster
-
autolysis
-
half-maximal
-
ca2+-activated
- phospholipid
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schneider
- phosphatidylinositol
- flies
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autolyzed
The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
calpain b, calpb, calpainb, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CALPB
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CAS REGISTRY NUMBER
COMMENTARY
78990-62-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-succinyl-L-Leu-L-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-L-Leu-L-Tyr + 7-amino-4-methyl-coumarin
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-
-
?
N-succinyl-Leu-Tyr-7-amido-4-methyl-coumarin + H2O
?
pH 7.5
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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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?
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
LITERATURE
Ca2+
Ca2+
Ca2+
activates calpain B, the enzyme undergoes N-terminal autolysis upon addition of Ca2+
Ca2+
a 6.4 mM free Ca2+ concentration is required for the half maximal activation of calpain B
Ca2+
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stimulation with Ca2+ results in autolytic conversion from the 104000 Da to a 81000 Da form with intermediary fragments. The two major products of autolysis appear at 96000 Da and 81000 Da
Ca2+
half-maximal activation at 3.28 mM for the soluble calpain B and 4.38 mM for the renatured calpain B
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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domain III might be the primary lipid binding site of calpain and may play a decisive role in orchestrating Ca2+- and lipid activation of the enzyme
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additional information
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no activation by phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol or phosphatidic acid. N-terminal autolysis in a Ca2+-dependent manner which runs parallel with the enzyme activation
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additional information
no activation by phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol or phosphatidic acid. N-terminal autolysis in a Ca2+-dependent manner which runs parallel with the enzyme activation
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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in the late embryos high activity is detected in the tracheas and their orifices as well as in the larynx
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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
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in the late embryos high activity is detected in the tracheas and their orifices as well as in the larynx
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activity is strongly detectable in follicular and border cells of the oocyte
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in the late embryos high activity is detected in the tracheas and their orifices as well as in the larynx
additional information
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calpain B is detectable in all developmental stages of the fly
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
in Schneider S2 cells, with increasing Ca2+ concentrations the enzyme adheres to intracellular membranes
with increasing Ca2+ concentrations the enzyme adheres to intracellular membranes
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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calpainB is required for acute myeloid leukemia 1-ETO-induced blood cell disorders in Drosophila
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
81000
estimated from amino acid sequence, activated enzyme after N-terminal autolysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
BIII-D613N/D614N
retains 30% of the wild-type Ca2+-binding capacity
BIII-D617N/D618
retains 60% of the wild-type Ca2+-binding capacity
BIII-E610A/D611A/P612A, delta613-620 deletion mutant
unable to bind Ca2+
BIII-E610Q/D611N/D613N/D614N
retains 16.2% of the wild-type Ca2+-binding capacity
BIII-E615Q/D616N/D617N/D618N
retains 36% of the wild-type Ca2+-binding capacity
BIII-P612A, delta613-620 deletion mutant
retains one-third of the original Ca2+- binding capacity
D613N/D614N
enhances specific activity to 114% of the wild-type activity
D617N/D618N
reduces specific activity to 66% of the wild-type activity
S845E
the mutation causes a small but reproducible increase in the activation of calpain B
T747E
the mutation causes a large increase in the activation of calpain B
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme Q73G/N74V/A75P/N223A/Q224V expressed in Escherichia coli
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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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Drosophila melanogaster (Q9VT65)
Jekely, G.; Friedrich, P.
Characterization of two recombinant Drosophila calpains. CALPA and a novel homolog, CALPB
J. Biol. Chem.
274
23893-23900
1999
Drosophila melanogaster, Drosophila melanogaster (Q9VT65)
Farkas, A.; Tompa, P.; Schad, E.; Sinka, R.; Jekely, G.; Friedrich, P.
Autolytic activation and localization in Schneider cells (S2) of calpain B from Drosophila
Biochem. J.
378
299-305
2003
Drosophila melanogaster
Tompa, P.; Emori, Y.; Sorimachi, H.; Suzuki, K.; Friedrich, P.
Domain III of calpain is a Ca2+-regulated phospholipid-binding domain
Biochem. Biophys. Res. Commun.
280
1333-1339
2001
Drosophila melanogaster
Friedrich, P.
The intriguing Ca2+ requirement of calpain activation
Biochem. Biophys. Res. Commun.
323
1131-1133
2004
Drosophila melanogaster (Q9VT65)
Friedrich, P.; Tompa, P.; Farkas, A.
The calpain-system of Drosophila melanogaster: coming of age
Bioessays
26
1088-1096
2004
Drosophila melanogaster (Q9VT65), Drosophila melanogaster
Alexa, A.; Bozky, Z.; Farkas, A.; Tompa, P.; Friedrich, P.
Contribution of distinct structural elements to activation of calpain by Ca2+ ions
J. Biol. Chem.
279
20118-20126
2004
Drosophila melanogaster (Q9VT65)
Kovacs, L.; Alexa, A.; Klement, E.; Kokai, E.; Tantos, A.; Gogl, G.; Sperka, T.; Medzihradszky, K.F.; Toezser, J.; Dombradi, V.; Friedrich, P.
Regulation of calpain B from Drosophila melanogaster by phosphorylation
FEBS J.
276
4959-4972
2009
Drosophila melanogaster (Q9VT65), Drosophila melanogaster
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