Thermodynamic Correlation with Kinetic Association Rates for Several Mutants of Mouse Acetylcholinesterase

摘要: Electrostatic forces play an important role in the association of cationic acetylcholine (ACh+) to the active site of acetylcholinesterase (AChE). Acetylcholinesterase has many negatively charged residues that are involved in the attraction of cationic ligands towards the catalytic site (1, 2). The turnover rate of this enzyme appears to be largely limited by the rate of diffusion (3). Many theoretical and experimental investigations have focused on the diffusional influence upon the rate of the overall enzymatic reaction.