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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

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

Volume 10, Issue 3, 2003

Page: [321 - 324] Pages: 4

DOI: 10.2174/0929866033478915

Price: $65

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.

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


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