EC Number |
Reaction |
Reference |
---|
3.1.1.47 | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate |
- |
- |
3.1.1.47 | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate |
Arg29 and Arg22 in the one monomer contribute to the catalytic competence of the active site across the dimer interface, and complement the catalytic triad of Ser47, Asp192, and His195 in the second monomer |
653704 |
3.1.1.47 | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate |
hydrolysis and inactivation of the lipid mediator platelet-activating factor PAF and/or oxidized phospholipids |
652609 |
3.1.1.47 | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate |
isozyme II of the enzyme also performs platelet-activating factor-dependent transacetylation, transfer of an acetyl group from platelet-activating factor to endogenous acceptor lipids |
652034 |
3.1.1.47 | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate |
mechanism |
651794 |
3.1.1.47 | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate |
mechanism, substrates can only bind in the aqueous phase to the active site of the plasma isozyme at the membrane-water interphase, catalytic triad is formed by Ser273, His351, and Asp296 |
653695 |
3.1.1.47 | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate |
stereochemistry |
650057 |
3.1.1.47 | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate |
the catalytic triad of the extracellular plasma enzyme form is of the alpha/beta-hydrolase type |
650326 |
3.1.1.47 | 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-alkyl-sn-glycero-3-phosphocholine + acetate |
the enzyme possesses both acetylhydrolase and transacetylase activities which remove PAF and its ether-linked analogues from LDL-particles upon LDL oxidation |
649713 |