Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.4 4.9
-
phosphatidylcholine constant water activity of 0.22 Sus scrofa
3.1.1.4 4.9
-
lysophosphatidylcholine constant water activity of 0.22 Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.1.1.4 toluene
-
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 oxidized phosphatidylcholine + H2O
-
Sus scrofa lysophosphatidylcholine + fatty acid
-
?
3.1.1.4 phosphatidylcholine + H2O
-
Sus scrofa 1-acylglycerophosphocholine + fatty acid
-
?
3.1.1.4 phospholipids + H2O
-
Sus scrofa ?
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.4 40
-
highest enzyme activity rate, but decrease of substrate occurs Sus scrofa