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Phase II Reactions: Acetylation Reactions

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Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
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The concept of prochirality leads to the nomenclature of the individual faces of a molecule and plays a crucial role in the enantioselective reaction. It is a concept where two or more achiral molecules react to produce chiral products. A typical process is the reaction of an achiral ketone to generate a chiral alcohol. Here, the achiral reactant reacts with an achiral reducing agent, sodium borohydride, to generate an equimolar mixture of the chiral enantiomers of the product. For example, an...

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

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Structural basis for acyl-group discrimination by human Gcn5L2.

Alison E Ringel¹, Cynthia Wolberger¹

¹Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.

Acta Crystallographica. Section D, Structural Biology

|July 6, 2016

Summary

Human Gcn5-related N-acetyltransferase 2 (Gcn5L2) shows reduced activity with longer acyl chains. Structural studies reveal how Gcn5L2 discriminates against larger acyl-CoA molecules, impacting its catalytic function.

Keywords:

Gcn5 acyltransferase butyryl-CoA histone acetyltransferase propionyl-CoA

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Last Updated: Mar 18, 2026

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Assays for Validating Histone Acetyltransferase Inhibitors

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

Area of Science:

Biochemistry
Molecular Biology
Epigenetics

Background:

Gcn5 is a crucial acetyltransferase regulating gene transcription via histone acetylation.
Recent findings reveal diverse lysine acyl modifications in vivo, prompting investigation into Gcn5's substrate specificity.

Purpose of the Study:

To examine the acyl-chain specificity of human Gcn5 (Gcn5L2).
To elucidate the structural mechanisms underlying Gcn5L2's discrimination between different acyl-CoA molecules.

Main Methods:

Biochemical assays to measure Gcn5L2 activity with varying acyl-CoA chain lengths.
X-ray crystallography to determine the structures of Gcn5L2 catalytic domain bound to propionyl-CoA and butyryl-CoA.

Main Results:

Gcn5L2 activity significantly decreases as acyl-chain length increases.
Structural analysis shows butyryl-CoA adopts a non-productive conformation in the active site, hindering lysine access.
Butyryl-CoA acts as a competitive inhibitor against acetyl-CoA.

Conclusions:

Gcn5L2 discriminates against longer acyl-CoA donors due to steric hindrance within the active site.
The observed structural mechanism explains Gcn5L2's preference for acetyl-CoA and its weak activity with larger acyl groups.