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Related Concept Videos

Oligosaccharide Assembly01:24

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.
Multiple sugar molecules that may or may...
Protein Glycosylation01:25

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...
Biosynthesis of Polysaccharides01:26

Biosynthesis of Polysaccharides

Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
Glucose Transporters01:27

Glucose Transporters

Glucose transporters facilitate the transport of glucose across the cell membrane. In addition to glucose, some glucose transporters can also aid the movement of other hexoses such as fructose, mannose, and galactose.
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes:
Proteoglycans01:05

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: Jun 12, 2026

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
12:29

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

Published on: March 11, 2022

Exploring genomes for glycosyltransferases.

Sara Fasmer Hansen1, Emmanuel Bettler, Asmund Rinnan

  • 1CERMAV-CNRS, University of Grenoble, F-38041 Grenoble cedex 9, France.

Molecular Biosystems
|June 18, 2010
PubMed
Summary
This summary is machine-generated.

Glycosyltransferases are diverse enzymes crucial for synthesizing complex carbohydrates. Bioinformatics methods like Hidden Markov Models aid in discovering new glycosyltransferase genes in genomes, particularly in plants.

More Related Videos

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Related Experiment Videos

Last Updated: Jun 12, 2026

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
12:29

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

Published on: March 11, 2022

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinformatics

Background:

  • Glycosyltransferases (GTs) represent a vast and diverse enzyme superfamily catalyzing glycosidic bond formation.
  • GTs are classified into families based on sequence similarity, maintained in the Carbohydrate Active enZyme database (CAZy).
  • The abundance of GT genes in an organism's genome correlates with the diversity of its cellular glycans; plants possess a disproportionately high number of GT genes.

Purpose of the Study:

  • To explore and identify novel glycosyltransferase genes within various genomes.
  • To evaluate the efficacy of advanced bioinformatics strategies for GT gene discovery.
  • To understand the genomic repertoire of GTs, especially in plants, due to their complex cell walls and secondary metabolites.

Main Methods:

  • Utilizing bioinformatics strategies for remote homology detection at 1D, 2D, and 3D levels.
  • Employing profile Hidden Markov Model (HMM) methods for sequence-based similarity detection.
  • Applying fold recognition techniques to identify GTs based on structural similarities.
  • Leveraging chemometric tools for analyzing large, complex genomic datasets and uncovering latent patterns.

Main Results:

  • Bioinformatics approaches, particularly the combination of HMMs and fold recognition, are effective for identifying GTs.
  • These methods facilitate the discovery of new GT genes in both bacterial and plant genomes.
  • Chemometric tools provide valuable insights into large-scale genomic data related to GTs.

Conclusions:

  • Advanced bioinformatics tools are essential for the comprehensive identification and characterization of glycosyltransferases.
  • The study highlights the utility of integrated computational approaches for exploring enzyme families like GTs.
  • Understanding the GT repertoire is key to deciphering glycan diversity, especially in plant systems.