ADP-GlcNAc

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• 英文名称: ADP-GlcNAc
• 英文别名: [(2R,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl] [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] hydrogen phosphate
• 化学式: C₁₈H₂₈N₆O₁₅P₂
• 分子量: 630.399
• InChiKey: BTEBOFHWUWYTHC-KSIRTVGVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.2
• 重原子数：
  41
• 可旋转键数：
  10
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  321
• 氢给体数：
  9
• 氢受体数：
  19

反应信息

• 作为产物：
  描述：

  N-acetylglucosamine-1-phosphate 、 5’-三磷酸腺苷 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8.5%的产率得到ADP-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.
• Exploiting Nucleotidylyltransferases To Prepare Sugar Nucleotides
  作者：Shannon C. Timmons、Roy H. Mosher、Sheryl A. Knowles、David L. Jakeman

  DOI：10.1021/ol0630853

  日期：2007.3.1

  Enzymatic approaches to prepare sugar nucleotides are gaining in importance and offer several advantages over chemical synthesis including high yields and stereospecificity. We report the cloning, expression, and purification of two new wild-type thymidylyltransferases and observed catalysis with a wide variety of substrates. Significant product inhibition was not observed with the enzymes studied over a 24 h period, enabling the efficient preparation of 15 sugar nucleotides, clearly demonstrating the synthetic utility of these biocatalysts.
• Probing the roles of conserved residues in uridyltransferase domain of Escherichia coli K12 GlmU by site-directed mutagenesis
  作者：Shuaishuai Wang、Xuan Fu、Yunpeng Liu、Xian-wei Liu、Lin Wang、Junqiang Fang、Peng George Wang

  DOI：10.1016/j.carres.2015.05.007

  日期：2015.9

  N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme that catalyzes both acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthesis pathway. Our previous study demonstrated that the uridyltransferase domain of GlmU (tGlmU) exhibited a flexible substrate specificity, which could be further applied in unnatural sugar nucleotides preparation. However, the structural basis of tolerating variant substrates is still not clear. Herein, we further investigated the roles of several highly conserved amino acid residues involved in substrate binding and recognition by structure-and sequence-guided site-directed mutagenesis. Out of total 16 mutants designed, tGlmU Q76E mutant which had a novel catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc was identified. Furthermore, tGlmU Y103F and N169R mutants were also investigated to have enhanced uridyltransferase activities compared with wide-type tGlmU. (C) 2015 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.