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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments

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Functional proteomic profiling of glycan-processing enzymes.

Keith A Stubbs¹, David J Vocadlo

¹Department of Chemistry, Simon Frasier University, Burnaby, British Columbia, Canada.

Methods in Enzymology

|November 23, 2006

Summary

Activity-based affinity probes help identify carbohydrate-processing enzymes involved in cellular functions and disease. These tools reveal multiple enzymes and aid in discovering new ones by profiling proteomes.

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Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry

Published on: April 21, 2017

Area of Science:

Biochemistry
Glycobiology
Proteomics

Background:

Glycoconjugates are crucial for cellular and organismal functions.
Understanding glycoconjugate regulation is key to deciphering their role in development and disease.
Enzymes processing glycoconjugates are essential targets for study.

Purpose of the Study:

To review the current state of activity-based affinity probes for profiling carbohydrate-processing enzymes.
To highlight the successes and limitations of these probes.
To discuss general design features and provide a specific example of exoglycosidase profiling.

Main Methods:

Utilizing activity-based affinity reagents to probe enzyme activity.
Simultaneously revealing multiple enzymes with similar functions.
Enriching proteomes of interest for enzyme identification and cloning.

Main Results:

Activity-based probes are effective tools for unraveling proteomes.
These probes facilitate the identification and cloning of novel carbohydrate-processing enzymes.
Profiling exoglycosidases from cell lysates demonstrates probe utility.

Conclusions:

Activity-based affinity probes are valuable for studying carbohydrate-processing enzymes.
These probes offer advantages in enzyme discovery and proteome analysis.
Further development and application of these probes will advance understanding of the 'glycocode'.