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Literature summary extracted from

  • Flesch, I.; Schmidt, B.; Ferber, E.
    Acylchain specificity and kinetic properties of phospholipase A1 and A2 of bone marrow-derived macrophages (1985), Z. Naturforsch. C, 40, 356-363.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.32 Ca2+
-
 Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.32 additional information
-
 additional information
-
 Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.32 Mus musculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.32 bone marrow
-
 Mus musculus
-
3.1.1.32 macrophage
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.32 1-palmitoyl-2-arachidonoylglycerophosphocholine + H2O
-
 Mus musculus palmitic acid + 2-arachidonoylglycerophosphocholine
-
 ?
3.1.1.32 1-palmitoyl-2-linoleoylglycerophosphocholine + H2O
-
 Mus musculus ?
-
 ?
3.1.1.32 1-palmitoyl-2-oleoylglycerophosphocholine + H2O
-
 Mus musculus palmitic acid + 2-oleoylglycerophosphocholine
-
 ?
3.1.1.32 additional information the enzyme exhibits both phospholipase A1 and phospholipase A2 activity Mus musculus ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.32 4 5
-
 Mus musculus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.32 3.5 4.5 pH 3.5: about 30% of maximal activity, pH 4.5: about 25% of maximal activity Mus musculus