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Human GlycoEnzymes and Related Genes

  • SUNY Buffalo

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

1 Scopus citations

Abstract

The human glycogenes constitute a family of ~350–450 proteins (~2%–3% of the human genome) that directly control the distribution of complex carbohydrate structures or glycans in mammalian cells. Many of these glycogenes are glycosyltransferases that facilitate the transfer of monosaccharides from activated nucleotide-sugar donors to carbohydrate acceptors. Additional enzymes participating in glycan biosynthesis include glycosidases, epimerases, transporters, sulfotransferases, and monosaccharide modifiers (kinases, dehydrogenases, structural proteins etc). Together these enzymes regulate the distribution of carbohydrates on the cell, i.e., the cellular glycome. This article lists the majority of these glycogenes and glycoenzymes, and describes their role in the biosynthesis of various classes of human cellular glycoconjugates.

Original languageEnglish
Title of host publicationEncyclopedia of Cell Biology
Subtitle of host publicationVolume 1-6, Second Edition
PublisherElsevier
Pages452-472
Number of pages21
Volume4
ISBN (Electronic)9780128216248
DOIs
StatePublished - Jan 1 2022

Keywords

  • Glycoenzyme
  • Glycolipid
  • Glycosaminoglycans
  • Glycoscience
  • Glycosidase
  • Glycosylation
  • Glycosyltransferase
  • GPI-linked
  • Heparan sulfate
  • Human
  • Mucin
  • N-linked glycans
  • O-linked glycans
  • Pathway maps
  • Sialic acid

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