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

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

Volume: 10 Issue: 3

Author(s): Jesse Oakes, Tina Nguyen and B. Mark Britt

Affiliation:

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

Abstract: Ellmans 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.

Cite this article as:

Oakes Jesse, Nguyen Tina and Britt Mark B., Arrhenius Analysis of the Electrophorus Electricus Acetylcholinesterase-Catalyzed Hydrolysis of Acetylthiocholine, Protein & Peptide Letters 2003; 10 (3) . https://dx.doi.org/10.2174/0929866033478915

DOI https://dx.doi.org/10.2174/0929866033478915	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305