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Updated: Jun 10, 2026

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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
Glycosyltransferases and their assays
1School of Pharmacy, University of East Anglia, Norwich, NR4 7TJ, UK.
Chembiochem : a European Journal of Chemical Biology
|July 31, 2010
Summary
Glycosyltransferases (GTs) are vital enzymes in biology, crucial for synthesizing complex carbohydrates. New bioassays are essential for studying GTs as drug targets and synthetic tools, especially fluorescence-based methods.
Area of Science:
- Biochemistry
- Enzymology
- Glycobiology
Background:
- Glycosyltransferases (GTs) are essential enzymes catalyzing the transfer of sugars to various acceptor molecules.
- Glycosylation reactions are fundamental to biological processes like cell adhesion and cell wall biosynthesis.
- GTs are significant targets in chemical biology and drug discovery, and valuable tools for synthesizing complex carbohydrates.
Purpose of the Study:
- To provide an overview of GT biochemistry and biology.
- To highlight the relevance of GTs in medicinal chemistry and chemical biology.
- To review recently developed GT bioassays, focusing on fluorescence-based assays.
Main Methods:
- Literature review of GT biochemistry and biology.
- Analysis of GT applications in medicinal chemistry and chemical biology.
- Survey of recently developed GT bioassay formats, emphasizing fluorescence-based methods.
Main Results:
- GTs play critical roles in fundamental biological processes and have broad applications.
- The identification of novel GTs necessitates robust and simple bioassays.
- Fluorescence-based assays represent a promising approach for GT detection and characterization.
Conclusions:
- GTs are important targets and tools in chemical biology and drug discovery.
- Development of efficient bioassays is crucial for understanding and utilizing GTs.
- Fluorescence-based bioassays offer a powerful platform for GT research.
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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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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.
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