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Arrhenius Analysis of the Electrophorus Electricus Acetylcholinesterase-Catalyzed Hydrolysis of Acetylthiocholine

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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.

Keywords: acetylthiocholine; electrophorus electricus acetylcholinesterase; ellmans method; scanning calorimetry

Document Type: Review Article


Publication date: June 1, 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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