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Glycosylation

Part 3. Proteomics

3.5. Proteome Diversity

Introductory Review

  1. Richard D. Cummings

Published Online: 15 JUL 2005

DOI: 10.1002/047001153X.g305106

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics

How to Cite

Cummings, R. D. 2005. Glycosylation. Encyclopedia of Genetics, Genomics, Proteomics and Bioinformatics.

Author Information

  1. University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA

Publication History

  1. Published Online: 15 JUL 2005

Abstract

Glycosylation is an enzymatic process in which sugars are added to other molecules to produce a glycosylated product. The major classes of enzymes that catalyze the process of glycosylation are transferases that use sugar nucleotide and lipid-linked sugar donors. Examples of the products of glycosylation reactions are glycoproteins, glycolipids, glycosaminoglycans, oligosaccharides, and polysaccharides. Glycosylation reactions occur in all animals, plants, fungi, and microorganisms. In animals, glycosylation reactions occur mainly in the cytoplasm, endoplasmic reticulum, Golgi apparatus, and the plasma membrane. Glycans are important in many aspects of cellular and developmental regulation, and defects in glycosylation in humans and animals result in developmental abnormalities and embryonic death. Glycosylation is a common and essential process in all organisms.

Keywords:

  • glycoprotein;
  • glycosylation;
  • glycoconjugate;
  • glycosyltransferase;
  • posttranslational modification;
  • glycan;
  • oligosaccharide;
  • polysaccharide