Cobra venom phospholipase A2: a review of its action toward lipid/water interfaces.
This review focuses on the mechanism of action of phospholipase A2 from cobra venom (Naja naja naja) toward the lipid/water interface. Particular points of interest include dramatic changes in the enzyme activity if the physical state of its substrate is altered and the activation of the enzyme by phosphorylcholine containing lipids. The experimental findings include the following: Micellar substrates are hydrolyzed faster by the enzyme than various bilayer forms of substrate aggregation. The activity of the enzyme toward short chain phospholipids increases suddenly above their critical micelle concentrations. An abrupt change in susceptibility to the enzyme is observed at the thermotropic phase transition of phospholipid vesicles. The enzyme shows the kinetic phenomena of surface dilution and activation by certain lipids, which suggest a two-step mechanism of action. A model is discussed which accommodates the present data both for the action of this enzyme at various lipid/water interfaces as well as its interaction with synthetic monomeric ligands and substrates.
D000818:Animals; D003902:Detergents; D004546:Elapid Venoms; D008024:Ligands; D008051:Lipid Bilayers; D009682:Magnetic Resonance Spectroscopy; D008823:Micelles; D017830:Octoxynol; D010740:Phospholipases / Q000378:metabolism*; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D010743:Phospholipids; D011092:Polyethylene Glycols; D013816:Thermodynamics; D014867:Water
D003902:Detergents; D004546:Elapid Venoms; D008024:Ligands; D008051:Lipid Bilayers; D008823:Micelles; D010743:Phospholipids; D014867:Water; D011092:Polyethylene Glycols; D017830:Octoxynol; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2