Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Acetylcholinesterase kinetics

P Hofer, U P Fringeli

Biophysics of Structure and Mechanism

|January 1, 1981

Summary

This summary is machine-generated.

Excess acetylcholine inhibits acetylcholinesterase (EC 3.1.1.7) primarily through a mechanism involving incomplete deacetylation of a ternary complex. This finding clarifies enzyme kinetics and substrate inhibition models.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Pediatric postmortem CT angiography: validation of vascular access for PMCT angiography in stillbirths, babies and toddlers.

Forensic science, medicine, and pathology·2023

Same author

Multi-energy reconstructions, central electron temperature measurements, and early detection of the birth and growth of runaway electrons using a versatile soft x-ray pinhole camera at MST.

The Review of scientific instruments·2021

Same author

[Medicolegal aspects of child abuse].

Der Radiologe·2016

Same author

Novel energy resolving x-ray pinhole camera on Alcator C-Mod.

The Review of scientific instruments·2012

Same author

Dynamic nuclear polarization at high magnetic fields in liquids.

Progress in nuclear magnetic resonance spectroscopy·2012

Same author

The impact of temperament in the course of alcohol dependence.

Journal of affective disorders·2011

Same journal

Transduction in photoreceptors: determination of the pigment transition or state coupled to excitation.

Biophysics of structure and mechanism·2012

Same journal

Upper limit on translational diffusion of visual pigment in intact unfixed barnacle photoreceptors.

Biophysics of structure and mechanism·2012

Same journal

Properties of the on-transient of the intracellular response in the barnacle photoreceptor.

Biophysics of structure and mechanism·2012

Same journal

Absorption of light by metarhodopsin modifies the effect of a conditioning light on the barnacle photoreceptor.

Biophysics of structure and mechanism·2012

Same journal

The effects of Mn2+ and Ca2+ on the prolonged depolarising after-potential in barnacle photoreceptor.

Biophysics of structure and mechanism·2012

Same journal

Blue adaptation: an experimental tool for the study of visual receptor mechanisms and behaviour of Drosophila.

Biophysics of structure and mechanism·2012

See all related articles

Area of Science:

Biochemistry
Enzyme kinetics

Background:

Acetylcholinesterase (AChE) plays a crucial role in neurotransmission by hydrolyzing acetylcholine.
Understanding AChE inhibition by excess substrate is vital for elucidating enzyme regulation.

Purpose of the Study:

To investigate and differentiate between proposed mechanisms of acetylcholinesterase inhibition by excess acetylcholine.
To determine the most accurate model describing experimental kinetic data.

Main Methods:

Mathematical modeling of three proposed inhibition mechanisms (substrate inhibition, ternary complex with complete/incomplete deacetylation, two-site mechanism).
Application of steady-state treatment and least-squares fitting to derive catalytic parameters.
Numerical integration to validate the steady-state approximation.

Related Experiment Videos

Main Results:

Mechanism (ii), involving a ternary complex with incomplete deacetylation, best describes the experimental data.
Specific rate constants were derived, and their limits were established.
The steady-state approximation is valid even for complex reaction mechanisms.

Conclusions:

The predominant mechanism for acetylcholinesterase inhibition by excess acetylcholine involves incomplete deacetylation.
Kinetic parameters provide insights into the enzyme's regulatory processes.
The study validates the use of steady-state approximations in complex enzyme kinetic analyses.