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 |
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 |
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 |
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 | - |
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 |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.4.22.B37 | 90134 | - |
x * 90134, calculation from nucleotide sequence | Drosophila melanogaster |
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 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.4.22.B37 | - |
Drosophila melanogaster |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
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 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.22.B37 | ? | x * 90134, calculation from nucleotide sequence | Drosophila melanogaster |