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Literature summary extracted from

  • Lichtenberg, D.; Romero, G.; Menashe, M.; Biltonen, R.L.
    Hydrolysis of dipalmitoylphosphatidylcholine large unilamellar vesicles by porcine pancreatic phospholipase A2 (1986), J. Biol. Chem., 261, 5334-5340.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.4 additional information reaction products like palmitoylphosphatidylcholine + palmitic acid do not have an activating effect under all experimental conditions, not essential Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.4 1,2-dipalmitoyl-phosphatidylcholine large unilamellar vesicles, inhibits hydrolysis of 1,2-dipalmitoyl-phosphatidylcholine small unilamellar vesicles Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.4 Ca2+ PLA2-binding is Ca2+-independent, PLA2-activation requires Ca2+ Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.4 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.4 pancreas
-
Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.4 1,2-dipalmitoyl-phosphatidylcholine + H2O
-
Sus scrofa 1-palmitoyl-glycerophosphorylcholine + palmitic acid
-
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