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Phase II Reactions: Acetylation Reactions

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Updated: Jun 26, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

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Published on: April 10, 2020

Protein acyl thioesterases (Review).

Ruth Zeidman¹, Caroline S Jackson, Anthony I Magee

¹Molecular Medicine, National Heart & Lung Institute, Sir Alexander Fleming Building, Imperial College London, London, UK.

Molecular Membrane Biology

|December 31, 2008

Summary

This summary is machine-generated.

Protein S-acylation dynamically regulates protein function. Protein thioesterase 1 (PPT1) is crucial for lysosomal degradation of S-acylated proteins, and its deficiency causes infant neuronal ceroid lipofuscinosis.

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Detection of Protein S-Acylation using Acyl-Resin Assisted Capture

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Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry

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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

S-acylation is a post-translational modification affecting protein localization and function.
Dynamic S-acylation occurs in vivo in response to stimuli.
Protein acyl transferases (PATs) and protein thioesterases (APTs) regulate S-acylation.

Purpose of the Study:

To elucidate the regulatory mechanisms of protein S-acylation and deacylation.
To differentiate the roles of protein thioesterase 1 (PPT1) and acyl-protein thioesterase 1 (APT1).

Main Methods:

Investigated the enzymatic processes of protein S-acylation and deacylation.
Examined the specific roles of APT1 and PPT1 in regulating S-acylation.
Studied the involvement of PPT1 in lysosomal degradation pathways.

Main Results:

APT1 regulates reversible S-acylation of cytoplasmic proteins in vivo.
PPT1 catalyzes the lysosomal degradation of S-acylated proteins.
PPT1 deficiency leads to infant neuronal ceroid lipofuscinosis.

Conclusions:

S-acylation is a dynamic regulatory process involving PATs and APTs.
APT1 and PPT1 have distinct roles in S-acylation regulation and protein degradation.
PPT1 is essential for lysosomal function and prevention of neurodegenerative disease.