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Abstract

N-Acetylglucosaminyltransferase-III (β-1,4-mannosyl-glycoprotein β1,4-N-acetylglu- cosaminyltransferase: EC 2.4.1.144) catalyzes the formation of a unique structure, bisecting GlcNAc, and is involved in the biosynthesis of complex and hybrid types of N-glycans. The addition of the bisecting GlcNAc residue to a core β-mannose by the enzyme prevents the actions of other GlcNAc transferases involved in the biosynthesis of multiantennary sugar chains, leading to a decrease in the branch formation of N-glycans. Because of this regulatory role, the enzyme has been considered to be a key glycosyltransferase in N-glycan biosynthesis. Relatively high levels of the activity were found in kidney and brain of mammals (Nishikawa et al. 1988a). Expression of GnT-III is enhanced during hepatocarcinogenesis, while the activity is nearly undetectable in normal liver (Narasimhan et al. 1988; Nishikawa et al. 1988b). Since expression of the enzyme appears to lead to a remarkable structural alteration of the sugar chains on the cell surface, it seems that the enzyme is associated with various biological events such as differentiation and carcinogenesis.

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© 2002 Springer Japan

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Ikeda, Y., Taniguchi, N. (2002). N-Acetylglucosaminyltransferase-III. In: Taniguchi, N., et al. Handbook of Glycosyltransferases and Related Genes. Springer, Tokyo. https://doi.org/10.1007/978-4-431-67877-9_11

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  • DOI: https://doi.org/10.1007/978-4-431-67877-9_11

  • Publisher Name: Springer, Tokyo

  • Print ISBN: 978-4-431-67996-7

  • Online ISBN: 978-4-431-67877-9

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