Home Why is the hydrolytic activity of acetylcholinesterase pH dependent? Kinetic study of acetylcholine and acetylthiocholine hydrolysis catalyzed by acetylcholinesterase from electric eel
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Why is the hydrolytic activity of acetylcholinesterase pH dependent? Kinetic study of acetylcholine and acetylthiocholine hydrolysis catalyzed by acetylcholinesterase from electric eel

  • Alena Komersová , Markéta Kovářová , Karel Komers , Václav Lochař EMAIL logo and Alexander Čegan
Published/Copyright: June 25, 2018
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Abstract

The dependence of the activity of acetylcholinesterase from electric eel at a pH value range of 4.8–9.8 (phosphate buffer), regarding acetylcholine and acetylthiocholine hydrolysis, was determined at 25 °C, ionic strength of 0.11 M, and initial substrate concentration of 4 mM. At a pH range of 4.8–9.8, the dependences A(pH) form a sigmoid increasing curve with the maximum catalytic activity at a pH range 8–9.5. For acetylcholine hydrolysis, the kinetic reason for such an increase in A consists mainly of an increase in the rate constant k2 (Michaelis-Menten) model with increasing pH of the reaction mixture. For acetylthiocholine hydrolysis, the kinetic explication of the determined dependence A(pH) is more complicated.

Funding source: Ministry of Education

Award Identifier / Grant number: SGS_2017_007

Funding statement: This work was supported by the Ministry of Education, Youth and Sports of the Czech Republic no. SGS_2017_007.

  1. Conflict of interest statement: The authors report no declarations of interest.

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Received: 2017-07-25
Revised: 2018-03-22
Accepted: 2018-04-16
Published Online: 2018-06-25
Published in Print: 2018-09-25

©2018 Walter de Gruyter GmbH, Berlin/Boston

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