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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.
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Oligosaccharide Assembly

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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Proteoglycans

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...

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Related Experiment Video

Updated: Jul 4, 2026

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility

Published on: March 11, 2022

Glycosyltransferases: structures, functions, and mechanisms.

L L Lairson¹, B Henrissat, G J Davies

¹Department of Chemistry, University of British Columbia, Vancouver, BC, Canada. llairson@scripps.edu

Annual Review of Biochemistry

|June 4, 2008

Summary

This summary is machine-generated.

Glycosyltransferases (GTs) are enzymes that form glycosidic bonds. Recent studies reveal new structural folds and mechanistic insights for GTs, particularly for retaining enzymes.

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Glycan Node Analysis: A Bottom-up Approach to Glycomics

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

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Last Updated: Jul 4, 2026

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility

Published on: March 11, 2022

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

Area of Science:

Biochemistry
Enzymology
Structural Biology

Background:

Glycosyltransferases (GTs) are crucial enzymes catalyzing glycosidic bond formation.
Two main structural folds (GT-A and GT-B) are known for nucleotide sugar-dependent GTs.
Emerging data reveals diverse folds for lipid phosphosugar-dependent GTs.

Purpose of the Study:

To elucidate the structural and mechanistic diversity of glycosyltransferases.
To provide new insights into the catalytic mechanisms of GTs, especially retaining enzymes.

Main Methods:

Structural analysis of enzyme domains.
Kinetic studies to probe reaction mechanisms.

Main Results:

Identified new structural folds beyond GT-A and GT-B for lipid-dependent GTs.
Inverting GTs employ an S(N)2-like mechanism with base catalysis.
GT-A fold enzymes utilize divalent cations, while GT-B enzymes use charged residues/dipoles for leaving group departure.
A mechanism involving a transient oxocarbenium ion intermediate is proposed for retaining GTs.

Conclusions:

Glycosyltransferase mechanisms exhibit significant diversity in both structure and catalysis.
The leaving phosphate group likely acts as a base catalyst in retaining GTs.