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Literature summary extracted from

  • Jekely, G.; Friedrich, P.
    Characterization of two recombinant Drosophila calpains. CALPA and a novel homolog, CALPB (1999), J. Biol. Chem., 274, 23893-23900.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.22.B36 phosphatidic acid activates Drosophila melanogaster
3.4.22.B36 phosphatidylinositol activates Drosophila melanogaster
3.4.22.B36 phosphatidylinositol 4,5-bisphosphate activates Drosophila melanogaster
3.4.22.B36 phosphatidylinositol 4-monophosphate activates Drosophila melanogaster
3.4.22.B37 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 Drosophila melanogaster

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.22.B36 expression of wild-type and truncated enzyme form, lacking the CALPA-specific unique insertion region Drosophila melanogaster
3.4.22.B37 expression in Escherichia coli Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
3.4.22.B36 additional information the truncated enzyme form lacking the CALPA-specific unique insertion region. Although it lacks the 16-amino acid long putative membrane-anchoring segment, its activation by phospholipids is similar to that of the full-length CALPA protein Drosophila melanogaster

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.22.B37 cytoplasm in Schneider S2 cells, with increasing Ca2+ concentrations the enzyme adheres to intracellular membranes Drosophila melanogaster 5737
-
3.4.22.B37 membrane with increasing Ca2+ concentrations the enzyme adheres to intracellular membranes Drosophila melanogaster 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.22.B36 Ca2+ activates, half-maximal activation of the full-length enzyme at 2.18 mM and for the truncated enzyme at 3.23 mM Drosophila melanogaster
3.4.22.B36 Mn2+ slight activation Drosophila melanogaster
3.4.22.B37 Ca2+ half-maximal activation at 3.28 mM for the soluble calpain B and 4.38 mM for the renatured calpain B Drosophila melanogaster

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.22.B37 90134
-
x * 90134, calculation from nucleotide sequence Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.B36 Drosophila melanogaster
-
-
-
3.4.22.B37 Drosophila melanogaster
-
-
-
3.4.22.B37 Drosophila melanogaster Q9VT65
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.22.B37
-
Drosophila melanogaster

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.B36 casein + H2O
-
Drosophila melanogaster hydrolyzed casein
-
?
3.4.22.B36 additional information the enzyme undergoes N-terminal autolysis in a Ca2+-dependent manner Drosophila melanogaster ?
-
?
3.4.22.B37 additional information N-terminal autolysis in a Ca2+-dependent manner which runs parallel with the enzyme activation Drosophila melanogaster ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.22.B37 ? x * 90134, calculation from nucleotide sequence Drosophila melanogaster