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Literature summary for 3.4.22.B36 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
Search for more literature for 3.4.22.B36

Activating Compound

Activating Compound Comment Organism Structure
phosphatidic acid activates Drosophila melanogaster
phosphatidylinositol activates Drosophila melanogaster
phosphatidylinositol 4,5-bisphosphate activates Drosophila melanogaster
phosphatidylinositol 4-monophosphate activates Drosophila melanogaster

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and truncated enzyme form, lacking the CALPA-specific unique insertion region Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
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

Metals/Ions

Metals/Ions Comment Organism Structure
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
Mn2+ slight activation Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
 Drosophila melanogaster hydrolyzed casein
-
 ?
additional information the enzyme undergoes N-terminal autolysis in a Ca2+-dependent manner Drosophila melanogaster ?
-
 ?