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首页> 外文期刊>Current Drug Targets >Structure, Expression, and Regulation of UDP-GlcNAc: Dolichol Phosphate GlcNAc-1-Phosphate Transferase (DPAGT1)
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Structure, Expression, and Regulation of UDP-GlcNAc: Dolichol Phosphate GlcNAc-1-Phosphate Transferase (DPAGT1)

机译:UDP-GlcNAc的结构,表达和调控:磷酸二氢甘醇GlcNAc-1-磷酸转移酶(DPAGT1)

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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).
机译:真核细胞蛋白质中天冬酰胺氨基酸上蛋白质的糖基化(与N相连)是由磷酸十二烷醇-焦磷酸和UDP-N-乙酰氨基葡糖的生物合成引发的。 UDP-GlcNAc:Dolhol Phosphate GlcNAc-1-Phosphate Transferase(DPAGT1)催化这种反应的酶在其基因,基因产物,膜拓扑,功能位点,脂质依赖性和代谢方面已在几种细胞类型中进一步表征规。这篇综述总结了这些特性,这是对Lehrman较早的详细和批判性评论的更新(Lehrman,M. A.(1991)Glycobiology,1,553-562)。

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  • 来源
    《Current Drug Targets》 |2009年第6期|p.477-482|共6页
  • 作者

    Roger K. Bretthauer;

  • 作者单位

    Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.;

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  • 正文语种 eng
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