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Literature summary extracted from

  • Dijkstra, B.W.; Renetseder, R.; Kalk, K.H.; Hol, W.G.J.; Drenth, J.
    Structure of porcine pancreatic phospholipase A2 at 2.6 A resolution and comparison with bovine phospholipase A2 (1983), J. Mol. Biol., 168, 163-179.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.4 2.6 resolution, R-factor of 0.241, 4295 reflections Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.4 Ca2+ two Ca2+ binding sites, first Ca2+ is strongly bound and essential for enzyme activity, the second binds more weakly and stabilizes interaction of two enzymes in crystal structure 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
-
?
-
?

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 phospholipids + H2O
-
Sus scrofa ?
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.4 monomer in solution PLA2 is a monomeric enzyme, no data concerning MW Sus scrofa