Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine.
Acetylcholinesterase from Electrophorus electricus was acetylated during the hydrolysis of [3H]acetylcholine and [3H]acetylthiocholine. The steady state levels of [3H]acetyl-enzyme were measured at different pH and different concentrations of substrate. The maximum acetylation fraction [S)----infinity) at pH 7.0 in 0.5 M salt was 0.65 with acetylcholine as substrate and 0.57 with acetylthiocholine as substrate. Acetylation is faster than deacetylation. The fraction of acetyl-enzyme was not affected by pH which indicates that acetylation and deacetylation are equally affected by changes in pH. This results supports the concept that acetylation and deacetylation involve similar mechanisms.
D000109:Acetylcholine / Q000378:metabolism*; D000110:Acetylcholinesterase / Q000378:metabolism*; D000122:Acetylthiocholine / Q000378:metabolism*; D000818:Animals; D002794:Choline / Q000031:analogs & derivatives*; D004557:Electric Organ / Q000201:enzymology; D004593:Electrophorus; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D011485:Protein Binding; D014316:Tritium
D014316:Tritium; D000122:Acetylthiocholine; D000110:Acetylcholinesterase; D002794:Choline; D000109:Acetylcholine