[Effect of environment on allosteric properties of acetylcholinesterase].
In the presence of organophosphorus inhibitors (OPI) AChE inhibition is initiated at a lower concentration of ACh; the plot reaction rate versus substrate concentration shows two maxima with a distinct minimum between them. It was shown that extremely mild conditions (short-term heating up to 50 degrees C; acidic or alkaline pH shift by 0.5 units; high concentrations of bivalent cations; erythrocyte storage) which do not affect substrate inhibition, remove this effect. The data obtained suggest that OPI effect is not directed to the site of AChE responsible for enzyme inhibition by ACh excess ("substrate inhibition site"), but to some other area. This results in a change in the conformation of the substrate inhibition site and a pronounced inhibition of the AChE activity takes place at lower substrate concentration.
D000110:Acetylcholinesterase / Q000097:blood*; D002413:Cations, Divalent; D002462:Cell Membrane / Q000201:enzymology; D002800:Cholinesterase Inhibitors; D004912:Erythrocytes / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D009943:Organophosphorus Compounds / Q000494:pharmacology*; D009994:Osmolar Concentration; D011487:Protein Conformation; D013048:Specimen Handling; D013696:Temperature
D002413:Cations, Divalent; D002800:Cholinesterase Inhibitors; D009943:Organophosphorus Compounds; D000110:Acetylcholinesterase
Vliianie usloviĭ sredy na allostericheskie svoĭstva atsetilkholinèsterazy.