多利醇
转移酶
生物化学
糖生物学
糖基化
化学
酶
磷酸盐
焦磷酸盐
天冬酰胺
糖基转移酶
生物合成
糖蛋白
聚糖
出处
期刊:Current Drug Targets
[Bentham Science]
日期:2009-06-01
卷期号:10 (6): 477-482
被引量:27
标识
DOI:10.2174/138945009788488369
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).
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