Turnover Number of Acetylcholinesterase

Turnover time of acetylcholinesterase.

The turnover time of the enzyme, acetylcholinesterase, is of biological interest because of the role proposed for its substrate in nerve conduction. According to the theory of Nachmansohn, the action of acetylcholine on a receptor protein is responsible for the generation of bioelectric potentials by increasing sodium conductance. Acetylcholinesterase, which inactivates acetylcholine by hydroly...

Turnover number of acetyl-cholinesterase.

The turnover number of acetylcholinesterase is of special interest because the enzyme is thought to be one of the fastest enzymes and because a high speed is a prerequisite for the role of the enzyme in nervous function (1). The earliest value of the turnover number was given by Rothenberg and Nachman sohn (2) in terms of the molecular weight for enzyme obtained from electric eel. The molecular...

Comparison of atypical and usual human serum cholinesterase. Purification, number of active sites, substrate affinity, and turnover number.

Atypical and usual human serum cholinesterases were purified and studied with the fluorescent probe, N-methyl-(7-dimethylcarbamoxy)quinolinium iodide. Four active sites per tetramer were found in each enzyme. The turnover numbers of usual and atypical cholinesterases were the same: 15,000 mumol of benzoylcholine hydrolyzed/min/mumol of active site; 48,000 min-1 for o-nitrophenylbutyrate; and 0....

Molecular dynamics of acetylcholinesterase.

Molecular dynamics simulations are leading to a deeper understanding of the activity of the enzyme acetylcholinesterase. Simulations have shown how breathing motions in the enzyme facilitate the displacement of substrate from the surface of the enzyme to the buried active site. The most recent work points to the complex and spatially extensive nature of such motions and suggests possible modes ...

Inhibitors of Acetylcholinesterase