UDP-fructose

• 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: UDP-fructose
• 英文别名: diphosphoric acid 1-β-D-fructofuranos-1-yl ester 2-uridin-5'-yl ester；UDP-(1)-fructose；[({[(2R,3S,4R,5R)-5-(2,4-dioxo-1,2,3,4-tetrahydropyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl)oxy]({[(2R,3S,4S,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)oxolan-2-yl]methoxy})phosphinic acid；[[(2R,3S,4R,5R)-5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2R,3S,4S,5R)-2,3,4-trihydroxy-5-(hydroxymethyl)oxolan-2-yl]methyl hydrogen phosphate
• 化学式: C₁₅H₂₄N₂O₁₇P₂
• 分子量: 566.306
• InChiKey: HIDNNWOFQMQOHD-HWEKWTFHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.9
• 重原子数：
  36
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.73
• 拓扑面积：
  292
• 氢给体数：
  9
• 氢受体数：
  17

反应信息

• 作为产物：
  描述：

  α-L-fucopyranosyl phosphate 、 尿苷-5'-三磷酸 在 Pyrococcus furious enzyme 、 magnesium 作用下， 以 various solvent(s) 为溶剂， 反应 1.0h， 生成 UDP-fructose
  参考文献：
  名称：

  One-Step Synthesis of Labeled Sugar Nucleotides for Protein O-GlcNAc Modification Studies by Chemical Function Analysis of an Archaeal Protein

  摘要：

  Herein we present the chemical function analysis of a recombinant sugar nucleotidyltransferase from the hyperthermophile Pyrococcus furiosus and its use in the one-pot synthesis of chloroacetyl- and alkyne-tagged analogues of uridinediphospho-N-acetylglucosamine (UDP-GlcNAc). The gene was originally annotated as a glucose-1-phosphate deoxythymidylyltransferase; however, kinetic analysis of a panel of sugar-1-phosphates with the protein shows that it is better described as a bifunctional protein that synthesizes UDP-GlcNAc from glucosamine-1-phosphate and acetyl coenzyme A (CoA). A new mass-spectrometry-based assay for the rapid analysis of the acyltransferase activity demonstrates that the enzyme can also accept cheaper truncated N-acetylcysteamine thioester substrates in place of the natural acetyl CoA. The enzyme can tolerate alkyne or chloride substitutions in the acyl moiety, thereby allowing the facile synthesis of tagged sugar nucleotides for future use in protein O-GlcNAc modification studies.

  DOI：

  10.1021/ja044117p

文献信息

• Structure−Activity Relationship of Uridine 5‘<b>-</b>Diphosphoglucose Analogues as Agonists of the Human P2Y₁₄ Receptor
  作者：Hyojin Ko、Ingrid Fricks、Andrei A. Ivanov、T. Kendall Harden、Kenneth A. Jacobson

  DOI：10.1021/jm061222w

  日期：2007.5.1

  moieties abolished activity; this is among the least permissive P2Y receptors. However, a 2-thiouracil modification in 15 (EC50 49 +/- 2 nM) enhanced the potency of UDPG (but not UDP-glucuronic acid) by 7-fold. 4-Thio analogue 13 was equipotent to UDPG, but S-alkylation was detrimental. Compound 15 was docked in a rhodposin-based receptor homology model, which correctly predicted potent agonism of UDP-fructose

  UDP葡萄糖（UDPG）及其衍生物是Gi蛋白偶联的P2Y14受体的天然激动剂，它存在于免疫系统中。我们合成并表征了在碱基，核糖和葡萄糖部分修饰的UDPG的药理学新类似物，作为结合建模设计新配体的基础。通过工程化的Galpha-q / i蛋白将在COS-7细胞中表达的重组人P2Y14受体与磷脂酶C偶联。尿嘧啶或核糖部分的大多数修饰废除了活性。这是最不被允许的P2Y受体之一。然而，在15（EC50 49 +/- 2 nM）中的2-硫尿嘧啶修饰将UDPG（而不是UDP-葡萄糖醛酸）的效力提高了7倍。4-硫代类似物13与UDPG等价，但是S-烷基化是有害的。化合物15停靠在基于罗丹蛋白的受体同源性模型中，该模型正确预测了UDP-果糖，UDP-甘露糖和UDP-肌醇的有效激动作用。UDPG的己糖部分与多个H键和带电荷的残基相互作用，并为激动剂修饰提供了肥沃的区域。
• One-Step Synthesis of Labeled Sugar Nucleotides for Protein <i>O</i>-GlcNAc Modification Studies by Chemical Function Analysis of an Archaeal Protein
  作者：Rahman M. Mizanur、Firoz A. Jaipuri、Nicola L. Pohl

  DOI：10.1021/ja044117p

  日期：2005.1.1

  Herein we present the chemical function analysis of a recombinant sugar nucleotidyltransferase from the hyperthermophile Pyrococcus furiosus and its use in the one-pot synthesis of chloroacetyl- and alkyne-tagged analogues of uridinediphospho-N-acetylglucosamine (UDP-GlcNAc). The gene was originally annotated as a glucose-1-phosphate deoxythymidylyltransferase; however, kinetic analysis of a panel of sugar-1-phosphates with the protein shows that it is better described as a bifunctional protein that synthesizes UDP-GlcNAc from glucosamine-1-phosphate and acetyl coenzyme A (CoA). A new mass-spectrometry-based assay for the rapid analysis of the acyltransferase activity demonstrates that the enzyme can also accept cheaper truncated N-acetylcysteamine thioester substrates in place of the natural acetyl CoA. The enzyme can tolerate alkyne or chloride substitutions in the acyl moiety, thereby allowing the facile synthesis of tagged sugar nucleotides for future use in protein O-GlcNAc modification studies.