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N-Acetylglucosaminyltransferase-VI

  • Koichi Honke
  • Naoyuki Taniguchi

Abstract

The biological roles of asparagine-linked oligosaccharides (N-glycans) on glycoproteins are thought to take place through the interaction of terminal glycan structures and their receptors. The diversity and avidity of the terminal structures, however, are regulated by the core structure of N-glycans (Schachter 1991). In vertebrates, six different N-acetylglucosaminyltransferases (GnT-I-VI) are involved in initiating the synthesis of highly branched N-glycan core structures (Fig. 1). GnT-VI catalyzes the transfer of GlcNAc to position four of the Manα1,6 arm of the core structure of N- glycan, forming the most highly branched pentaantennary glycans with a bisecting GlcNAc. These glycans have been found in hen ovomucoid (Yamashita et al. 1982; Paz Parente et al. 1982) and fish egg glycoprotein (Taguchi et al. 1995).
Fig. 1

Structure of pentaantennary N-linked oligosaccharide with the bisecting GlcNAc

Keywords

GlcNAc Residue Terminal Structure Yellow Brick Road Biantennary Oligosaccharide Bisect GlcNAc Residue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Koichi Honke
    • 1
  • Naoyuki Taniguchi
    • 1
  1. 1.Department of BiochemistryOsaka University Medical SchoolSuitaJapan

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