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Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

Phase II Reactions: Acetylation Reactions

Phase II Reactions: Acetylation Reactions

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.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...

Amines to Amides: Acylation of Amines

Amines to Amides: Acylation of Amines

Various carboxylic acid derivatives (such as acid chlorides, esters, and anhydrides) can be used for the acylation of amines to yield amides. The reaction requires two equivalents of amines. The first amine molecule functions as a nucleophile and attacks the carbonyl carbon to produce a tetrahedral intermediate. This is followed by the loss of the leaving group and restoration of the C=O bond.
Next, the second equivalent of amine serves as a Brønsted base and deprotonates the quaternary amide...

Protein Glycosylation

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...

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Related Experiment Video

Updated: Jul 5, 2026

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

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

Published on: April 10, 2020

Analysis of protein acylation.

C S Jackson¹, A I Magee

¹National Institute for Medical Research, London, United Kingdom.

Current Protocols in Protein Science

|April 23, 2008

Summary

This study details methods for labeling eukaryotic cells with radiolabeled fatty acids, like myristate and palmitate. Analysis techniques are provided to identify protein acylation and bound fatty acids.

Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Protein acylation involves attaching fatty acids, such as myristate and palmitate, to proteins.
This modification plays a crucial role in protein function and localization within eukaryotic cells.

Purpose of the Study:

To describe protocols for labeling eukaryotic cells using radiolabeled fatty acids.
To outline methods for analyzing protein acylation, including fatty acid linkage and identification.

Main Methods:

Utilizing radiolabeled myristate (14:0) and palmitate (16:0) for in vitro labeling of eukaryotic cells.
Employing various analytical techniques to determine the nature of fatty acid linkages to proteins.
Assessing potential interconversion of fatty acids bound to proteins.

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

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

Published on: April 9, 2021

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

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Last Updated: Jul 5, 2026

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

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

Published on: April 10, 2020

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

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

Published on: April 9, 2021

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry

Published on: April 4, 2018

Main Results:

Successful labeling of eukaryotic cells with radiolabeled fatty acids.
Established methods for characterizing protein-bound fatty acids and their linkages.
Demonstrated ability to identify specific protein-bound fatty acids.

Conclusions:

Provides a comprehensive set of protocols for studying protein acylation in eukaryotic cells.
Enables detailed analysis of fatty acid modifications on proteins.
Facilitates the identification of proteins undergoing myristoylation and palmitoylation.