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

被引：25

作者：

Bretthauer, Roger K. ^{[1
]}

机构：

[1] Univ Notre Dame, Dept Chem & Biochem, Notre Dame, IN 46556 USA

来源：

CURRENT DRUG TARGETS | 2009年 / 10卷 / 06期

关键词：

N-ACETYLGLUCOSAMINYLPYROPHOSPHORYL POLYPRENOLS; ACETYL-D-GLUCOSAMINE; HAMSTER OVARY CELLS; PROTEIN GLYCOSYLATION; N-ACETYLGLUCOSAMINE-1-PHOSPHATE TRANSFERASE; ENDOPLASMIC-RETICULUM; HORMONAL-REGULATION; MOLECULAR-CLONING; BIOSYNTHESIS; GENE;

D O I：

10.2174/138945009788488369

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

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).

引用

页码：477 / 482

页数：6

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