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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....

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Related Experiment Video

Updated: Feb 18, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Global substrate specificity profiling of post-translational modifying enzymes.

Sam L Ivry^1,2, Nicole O Meyer¹, Michael B Winter¹

¹Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California.

Protein Science : a Publication of the Protein Society

|November 24, 2017

Summary

Identifying enzyme substrates is key to understanding cellular signaling and disease. Peptide libraries, like our multiplex substrate profiling by mass spectrometry (MSP-MS) assay, help determine post-translational modifying (PTM) enzyme specificity.

Keywords:

kinases mass spectrometry peptide libraries peptide synthesis post-translation modifying enzymes proteases substrate specificity

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Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Published on: November 7, 2019

Related Experiment Videos

Last Updated: Feb 18, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Published on: November 7, 2019

Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Post-translational modifying (PTM) enzymes regulate cellular signaling pathways.
Understanding PTM enzyme substrate specificity is crucial for elucidating biological functions in health and disease.

Purpose of the Study:

To review peptide-based approaches for analyzing PTM enzyme substrate specificity.
To highlight the application of these methods, particularly multiplex substrate profiling by mass spectrometry (MSP-MS), for PTM enzyme research.

Main Methods:

Utilizing peptide chemistry to generate diverse peptide libraries.
Employing multiplex substrate profiling by mass spectrometry (MSP-MS) with rationally designed tetradecapeptides.
Applying these methods to proteases and kinases to determine substrate specificity.

Main Results:

Peptide-based approaches enable rapid querying of PTM enzyme substrate recognition.
The MSP-MS assay effectively identifies substrate specificities for various PTM enzymes.
This information aids in uncovering biological functions and designing substrates and inhibitors.

Conclusions:

Peptide libraries are powerful tools for PTM enzyme research.
The MSP-MS assay provides a robust method for substrate specificity determination.
Combining techniques offers a systems-level understanding of PTM enzyme regulation.