dUDP-GlcNAc | 1222974-30-2

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘧啶核苷酸
• 英文名称: dUDP-GlcNAc
• 英文别名: [(2R,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl] [[(2R,3S,5R)-5-(2,4-dioxopyrimidin-1-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] hydrogen phosphate
• CAS: 1222974-30-2
• 化学式: C₁₇H₂₇N₃O₁₆P₂
• 分子量: 591.359
• InChiKey: NDDZEZXRDWJGBF-RPFYLOLLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -5.7
• 重原子数：
  38
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  280
• 氢给体数：
  8
• 氢受体数：
  16

反应信息

• 作为产物：
  描述：

  N-acetylglucosamine-1-phosphate 、 脱氧尿苷 5'-三磷酸酯 在 recombinant N-acetylglucosamine-1-phosphate uridyltransferase-Tr₂₂₉ from Escherichia coli K₁₂ 、 sodium chloride 、 magnesium chloride 、 1,4-二巯基-2,3-丁二醇 、 BSA 作用下， 反应 0.5h， 以57.6%的产率得到dUDP-GlcNAc
  参考文献：
  名称：

  Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12

  摘要：

  N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Escherichia coli K12 is a bifunctional enzyme that catalyzes both the acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthetic pathway. In this study, we report the broad substrate specificity of the pyrophosphorylase domain of GlmU during its uridyltransfer reaction and the substrate priority is ranked in the following order: UTP > dUTP > dTTP >> CTP > dATP/dm(6) ATP. This pyrophosphorylase domain of GlmU is also a tool to synthesize UDP-GlcNAc analogs, two examples of which were synthesized herein in multiple mg scale in vitro. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2009.09.039

文献信息

• Systematic study on the broad nucleotide triphosphate specificity of the pyrophosphorylase domain of the N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli K12
  作者：Junqiang Fang、Wanyi Guan、Li Cai、Guofeng Gu、Xianwei Liu、Peng George Wang

  DOI：10.1016/j.bmcl.2009.09.039

  日期：2009.11

  N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Escherichia coli K12 is a bifunctional enzyme that catalyzes both the acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthetic pathway. In this study, we report the broad substrate specificity of the pyrophosphorylase domain of GlmU during its uridyltransfer reaction and the substrate priority is ranked in the following order: UTP > dUTP > dTTP >> CTP > dATP/dm(6) ATP. This pyrophosphorylase domain of GlmU is also a tool to synthesize UDP-GlcNAc analogs, two examples of which were synthesized herein in multiple mg scale in vitro. (C) 2009 Elsevier Ltd. All rights reserved.
• Investigation of the nucleotide triphosphate substrate specificity of Homo sapiens UDP-N-acetylgalactosamine pyrophosphorylase (AGX1)
  作者：Mengyang Xue、Wanyi Guan、Yang Zou、Junqiang Fang、Xian-wei Liu、Peng George Wang、Fengshan Wang

  DOI：10.1016/j.bmcl.2012.04.102

  日期：2012.6

  Nucleotide sugars are essential glycosyl donors for Leloir-type glycosyltransferases. The UDP-N-acetylgalactosamine pyrophosphorylase (UDP-GalNAc PP; AGX1) from Homo sapiens catalyzes the synthesis of UDP-N-acetylgalactosamine from N-acetylgalactosamine 1-phosphate and UTP. In this Letter, we systematically studied nucleotide substrate specificity of AGX1 during its uridyltransfer reaction, and described the capability of AGX1 to catalyze dUTP and dTTP to their corresponding nucleotide sugars for the first time. Furthermore, using such a eukaryotic enzyme, we synthesized dUDP-GalNAc and dTDP-GalNAc in multiple mg scale in vitro efficiently and rapidly. Crown Copyright (C) 2012 Published by Elsevier Ltd. All rights reserved.
• A chemoenzymatic route to synthesize unnatural sugar nucleotides using a novel N-acetylglucosamine-1-phosphate pyrophosphorylase from Camphylobacter jejuni NCTC 11168
  作者：Junqiang Fang、Mengyang Xue、Guofeng Gu、Xian-wei Liu、Peng George Wang

  DOI：10.1016/j.bmcl.2013.06.003

  日期：2013.8

  A novel N-acetylglucosamine-1-phosphate pyrophosphorylase was identified from Campylobacter jejuni NCTC 11168. An unprecedented degree of substrate promiscuity has been revealed by systematic studies on its substrate specificities towards sugar-1-P and NTP. The yields of the synthetic reaction of seven kinds of sugar nucleotides catalyzed by the enzyme were up to 60%. In addition, the yields of the other nine were around 20%. With this enzyme, three novel sugar nucleotide analogs were synthesized on a preparative scale and well characterized. (C) 2013 Elsevier Ltd. All rights reserved.