Abstract
Asparagine-linked glycosylation is a covalent modification of secretory and integral membrane proteins in eukaryotes that modulates the structure and function of these proteins. Dolichol-linked oligosaccharides are transferred en bloc to selected asparagine residues of nascent polypeptides. Biosynthesis of the dolichol-bound oligosaccharides is initiated by formation of GlcNAc-P-P-dolichol from UDP-GlcNAc and dolichol phosphate. This reaction is catalyzed by the endoplasmic reticulum (ER) residential enzyme UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1- phosphate transferase (GPT). The two substrates, dolichol phosphate and UDP- GlcNAc, can serve other pathways, but the product of GPT activity can only participate in lipid-bound oligosaccharide biosynthesis. Thus, GPT catalyzes the committed step of the dolichol cycle involved in asparagine-linked glycosylation.
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© 2002 Springer Japan
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Hübel, A., Schwarz, R.T. (2002). Dolichol Phosphate GlcNAc-1-P Transferase. In: Taniguchi, N., et al. Handbook of Glycosyltransferases and Related Genes. Springer, Tokyo. https://doi.org/10.1007/978-4-431-67877-9_80
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DOI: https://doi.org/10.1007/978-4-431-67877-9_80
Publisher Name: Springer, Tokyo
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