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Literature summary extracted from

  • Yu, B.Z.; Pan, Y.H.; Janssen, M.J.; Bahnson, B.J.; Jain, M.K.
    Kinetic and structural properties of disulfide engineered phospholipase A2: insight into the role of disulfide bonding patterns (2005), Biochemistry, 44, 3369-3379.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.4 wild-type and mutant A12T/H15D/M20L/E71N, in ligand-free form and in complex with inhibitor MJ33 Sus scrofa

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.4 A12T/H15D/M20L/E71N catalytic activity similar to wild-type Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.4 1-hexadecyl-3-(trifluoroethyl)-sn-glycero-2-phosphomethanol i.e. MJ33 Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.4 0.2
-
phosphatidylcholine mutant A12T/H15D/M20L/E71N, pH 8.0, 24°C Sus scrofa
3.1.1.4 0.2
-
phosphatidylcholine wild-type, pH 8.0, 24°C Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.4 Sus scrofa P00592 isoform IB PLA”
-

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 phosphatidylcholine + H2O
-
Sus scrofa 1-acylglycerophosphocholine + fatty acid
-
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Synonyms

EC Number Synonyms Comment Organism
3.1.1.4 IB PLA2
-
Sus scrofa