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Literature summary for 3.1.1.4 extracted from

  • Egger, D.; Wehtje, E.; Adlercreutz, P.
    Characterization and optimation of phospholipase A2 catalyzed synthesis of phosphatidylcholine (1997), Biochim. Biophys. Acta, 1343, 76-84.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.9
-
phosphatidylcholine constant water activity of 0.22 Sus scrofa
4.9
-
lysophosphatidylcholine constant water activity of 0.22 Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phospholipids + H2O Sus scrofa
-
?
-
?

Organic Solvent Stability

Organic Solvent Comment Organism
toluene
-
Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxidized phosphatidylcholine + H2O
-
Sus scrofa lysophosphatidylcholine + fatty acid
-
?
phosphatidylcholine + H2O
-
Sus scrofa 1-acylglycerophosphocholine + fatty acid
-
?
phospholipids + H2O
-
Sus scrofa ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
highest enzyme activity rate, but decrease of substrate occurs Sus scrofa