Arrhenius Analysis of the Electrophorus Electricus Acetylcholinesterase-Catalyzed Hydrolysis of Acetylthiocholine
Ellman's method was used to determine the Michaelis-Menten parameters for the hydrolysis of acetylthiocholine by Electrophorus electricus acetylcholinesterase from 12 to 37°C. Arrhenius analysis revealed that the activation energy for formation of the enzyme / substrate complex is 22.2 ± 1.1 kJ / mole. The Arrhenius plot of kcat is markedly curved and attributed to comparable rates of acylation and deacylation due to the absence of evidence for a temperature-dependent enzyme conformational change by differential scanning calorimetry.
Document Type: Review Article
Publication date: June 1, 2003
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