5-(2-Furyl)-UDP-alpha-D-galactose | 1242712-30-6

• 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: 5-(2-Furyl)-UDP-alpha-D-galactose
• 英文别名: [[(2R,3S,4R,5R)-5-[5-(furan-2-yl)-2,4-dioxopyrimidin-1-yl]-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2R,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl] hydrogen phosphate
• CAS: 1242712-30-6
• 化学式: C₁₉H₂₆N₂O₁₈P₂
• 分子量: 632.366
• InChiKey: NYZDFCGXVFREHX-SCPZDFDFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -5.9
• 重原子数：
  41
• 可旋转键数：
  10
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  305
• 氢给体数：
  9
• 氢受体数：
  18

反应信息

• 作为产物：
  描述：

  5-(furan-2-yl)uridine-5′-triphosphate 、 半乳糖-1-磷酸 在 尿苷(5')二氢二磷酰(1)-alpha-D-葡萄糖 、 无机焦磷酸酶 、 galactose-1-phosphate uridylyltransferase 、 glucose-1-phosphate uridylyltransferase 作用下， 以 aq. buffer 为溶剂， 反应 24.0h， 生成 5-(2-Furyl)-UDP-alpha-D-galactose
  参考文献：
  名称：

  Enzymatic synthesis of nucleobase-modified UDP-sugars: scope and limitations

  摘要：

  Glucose-1-phosphate uridylyltransferase in conjunction with UDP-glucose pyrophosphorylase was found to catalyse the conversion of a range of 5-substituted UTP derivatives into the corresponding UDP-galactose derivatives in poor yield. Notably the 5-iodo derivative was not converted to UDP-sugar. In contrast, UDP-glucose pyrophosphorylase in conjunction with inorganic pyrophosphatase was particularly effective at converting 5-substituted UTP derivatives, including the iodo compound, into a range of gluco-configured 5-substituted UDP-sugar derivatives in good yields. Attempts to effect 400-epimerization of these 5-substituted UDP-glucose with UDP-glucose 4 ''-epimerase from yeast were unsuccessful, while use of the corresponding enzyme from Erwinia amylovora resulted in efficient epimerization of only 5-iodo-UDP-Glc, but not the corresponding 5-aryl derivatives, to give 5-iodo-UDP-Gal. Given the established potential for Pd-mediated cross-coupling of 5-iodo-UDP-sugars, this provides convenient access to the galacto-configured 5-substituted-UDP-sugars from gluco-configured substrates and 5-iodo-UTP. (C) 2015 The Authors. Published by Elsevier Ltd.

  DOI：

  10.1016/j.carres.2014.12.005

文献信息

• A Novel Fluorescent Probe for Retaining Galactosyltransferases
  作者：Thomas Pesnot、Monica M. Palcic、Gerd K. Wagner

  DOI：10.1002/cbic.201000013

  日期：——

  A new U: A new fluorescent derivative of UDP‐galactose, modified at the uracil base, is strongly emissive in aqueous solution. The fluorescence emission is quenched upon specific binding at a galactosyltransferase. This effect was exploited for ligand‐displacement experiments with four different enzymes.

  一个新的U：在尿嘧啶碱基上修饰的一种新的UDP-半乳糖的荧光衍生物，在水溶液中强烈发射。在半乳糖基转移酶上特异性结合后，荧光发射被猝灭。这种作用被用于四种不同酶的配体置换实验。
• Enzymatic synthesis of nucleobase-modified UDP-sugars: scope and limitations
  作者：Ben A. Wagstaff、Martin Rejzek、Thomas Pesnot、Lauren M. Tedaldi、Lorenzo Caputi、Ellis C. O’Neill、Stefano Benini、Gerd K. Wagner、Robert A. Field

  DOI：10.1016/j.carres.2014.12.005

  日期：2015.3

  Glucose-1-phosphate uridylyltransferase in conjunction with UDP-glucose pyrophosphorylase was found to catalyse the conversion of a range of 5-substituted UTP derivatives into the corresponding UDP-galactose derivatives in poor yield. Notably the 5-iodo derivative was not converted to UDP-sugar. In contrast, UDP-glucose pyrophosphorylase in conjunction with inorganic pyrophosphatase was particularly effective at converting 5-substituted UTP derivatives, including the iodo compound, into a range of gluco-configured 5-substituted UDP-sugar derivatives in good yields. Attempts to effect 400-epimerization of these 5-substituted UDP-glucose with UDP-glucose 4 ''-epimerase from yeast were unsuccessful, while use of the corresponding enzyme from Erwinia amylovora resulted in efficient epimerization of only 5-iodo-UDP-Glc, but not the corresponding 5-aryl derivatives, to give 5-iodo-UDP-Gal. Given the established potential for Pd-mediated cross-coupling of 5-iodo-UDP-sugars, this provides convenient access to the galacto-configured 5-substituted-UDP-sugars from gluco-configured substrates and 5-iodo-UTP. (C) 2015 The Authors. Published by Elsevier Ltd.