N-Trifluoroacetyl-O-phosphoryl-6-amino-1-hexanol | 40248-29-1

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磷酸及其衍生物
• 英文名称: N-Trifluoroacetyl-O-phosphoryl-6-amino-1-hexanol
• 英文别名: 6-trifluoroacetamido-hexyl-1-phosphate；N-Trifluoracetyl-6-amino-1-hexanolphosphat；6-[(2,2,2-Trifluoroacetyl)amino]hexyl dihydrogen phosphate
• CAS: 40248-29-1
• 化学式: C₈H₁₅F₃NO₅P
• 分子量: 293.18
• InChiKey: GNZCBSOZNCYWRW-UHFFFAOYSA-N

物化性质

• 密度：
  1.406±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.3
• 重原子数：
  18
• 可旋转键数：
  8
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  95.9
• 氢给体数：
  3
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  N-Trifluoroacetyl-O-phosphoryl-6-amino-1-hexanol 在 ammonium hydroxide 、 三正丁胺 作用下， 以 吡啶 、 N,N-二甲基甲酰胺 为溶剂， 反应 3.5h， 生成 GDP-Hexanolamine
  参考文献：
  名称：

  An Improved Method for the Synthesis of Gdp-Hexanolamine Derivatives, key Reagents for the Purification and Characterisation of Carbohydrate Processing Enzymes

  摘要：

  As part of our ongoing studies on the isolation and characterisation of alpha-(1,3)-fucosyltransferase (FucT) enzymes, an improved method for the synthesis and purification of the key biological tool GDP-hexanolamine (1a), together with detailed experimental conditions and product characterisation are reported. We demonstrate the viability of the product obtained, by its competitive inhibition of an alpha-(1,3)-fucosyltransferase. Subsequently, we are able to use it to derivatise a sepharose gel column which we show is highly efficient in the purification of a recombinant alpha-(1,3)-fucosyltransferase from a crude preparation. The GDP-hexanolamine is converted to the photoaffinity probe GDP-hexanolaminyl-4-azidosalicylate (1b), useful in the characterisation of fucosyltransferase enzymes.

  DOI：

  10.1080/07328309608005688
• 作为产物：
  描述：

  乙基三氟巯基乙酯 、 6-氨基己基二氢磷酸酯 在 lithium hydroxide 作用下， 以 丙酮 为溶剂， 反应 2.5h， 以95%的产率得到N-Trifluoroacetyl-O-phosphoryl-6-amino-1-hexanol
  参考文献：
  名称：

  An Improved Method for the Synthesis of Gdp-Hexanolamine Derivatives, key Reagents for the Purification and Characterisation of Carbohydrate Processing Enzymes

  摘要：

  As part of our ongoing studies on the isolation and characterisation of alpha-(1,3)-fucosyltransferase (FucT) enzymes, an improved method for the synthesis and purification of the key biological tool GDP-hexanolamine (1a), together with detailed experimental conditions and product characterisation are reported. We demonstrate the viability of the product obtained, by its competitive inhibition of an alpha-(1,3)-fucosyltransferase. Subsequently, we are able to use it to derivatise a sepharose gel column which we show is highly efficient in the purification of a recombinant alpha-(1,3)-fucosyltransferase from a crude preparation. The GDP-hexanolamine is converted to the photoaffinity probe GDP-hexanolaminyl-4-azidosalicylate (1b), useful in the characterisation of fucosyltransferase enzymes.

  DOI：

  10.1080/07328309608005688

文献信息

• Syntheses of inhibitors for the enzyme thymidine 5′-diphosphate-glucose-4,6-dehydratase (EC 4.2.1.46)
  作者：Andreas Naundorf、Werner Klaffke

  DOI：10.1016/s0008-6215(99)00074-9

  日期：1999.5

  Inhibitors of the enzyme thymidine 5'-diphosphate-glucose-4,6-dehydratase (EC 4.2.1.46) were synthesised starting from thymidine, 2-deoxy-uridine and -cytidine. The diphosphate moieties have either been replaced by methylene diphosphonate or phosphoryl hydroxyacetic acid to yield inhibitors in a similar range to thymidine 5'-diphosphate itself. Spacers were attached to various positions, of which those at C-5 of the nucleobase were suitable analogues and showed a mixed type of inhibition characteristics, whereas attachment at other sites led to marginally active or inactive inhibitors. These investigations will prepare the ground for developing a purification procedure based on affinity chromatography. (C) 1999 Elsevier Science Ltd. All rights reserved.
• An Improved Method for the Synthesis of Gdp-Hexanolamine Derivatives, key Reagents for the Purification and Characterisation of Carbohydrate Processing Enzymes
  作者：Mark Bamford、Christopher Britten、Eleanor Draeger、Paul Gore、Duncan S. Holmes

  DOI：10.1080/07328309608005688

  日期：1996.8

  As part of our ongoing studies on the isolation and characterisation of alpha-(1,3)-fucosyltransferase (FucT) enzymes, an improved method for the synthesis and purification of the key biological tool GDP-hexanolamine (1a), together with detailed experimental conditions and product characterisation are reported. We demonstrate the viability of the product obtained, by its competitive inhibition of an alpha-(1,3)-fucosyltransferase. Subsequently, we are able to use it to derivatise a sepharose gel column which we show is highly efficient in the purification of a recombinant alpha-(1,3)-fucosyltransferase from a crude preparation. The GDP-hexanolamine is converted to the photoaffinity probe GDP-hexanolaminyl-4-azidosalicylate (1b), useful in the characterisation of fucosyltransferase enzymes.