Structure, Expression, and Regulation of UDP-GlcNAc: Dolichol Phosphate GlcNAc-1-Phosphate Transferase (DPAGT1)

Author(s): Roger K. Bretthauer.

Journal Name: Current Drug Targets

Volume 10 , Issue 6 , 2009

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Abstract:

Glycosylation of proteins on asparagine amino acids (N-linked) in proteins of eukaryotic cells is initiated by the biosynthesis of dolichol-pyrophosphate-N-acetylglucosamine from dolichol-phosphate and UDP-N-acetylglucosamine. The enzyme catalyzing this reaction, UDP-GlcNAc:Dolichol Phosphate GlcNAc-1-Phosphate Transferase (DPAGT1), has been further characterized in several cell types with respect to its gene, gene products, membrane topology, functional sites, lipid dependence, and metabolic regulation. This review summarizes these properties as an update from an earlier detailed and critical review by Lehrman (Lehrman, M. A. (1991) Glycobiology, 1, 553-562).

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Article Details

VOLUME: 10
ISSUE: 6
Year: 2009
Page: [477 - 482]
Pages: 6
DOI: 10.2174/138945009788488369
Price: $58

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