diethyl (5-formyl-6-hydroxy-2-naphthyl)phosphate | 882424-42-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: diethyl (5-formyl-6-hydroxy-2-naphthyl)phosphate
• 英文别名: Diethyl (5-formyl-6-hydroxynaphthalen-2-yl) phosphate
• CAS: 882424-42-2
• 化学式: C₁₅H₁₇O₆P
• 分子量: 324.27
• InChiKey: BTFUTONEXVFCAU-UHFFFAOYSA-N

物化性质

• 沸点：
  430.0±38.0 °C(Predicted)
• 密度：
  1.328±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  22
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  82.1
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  diethyl (5-formyl-6-hydroxy-2-naphthyl)phosphate 在 三甲基溴硅烷 、 水 作用下， 以 二氯甲烷 、 乙醚 为溶剂， 反应 3.0h， 以20%的产率得到5-Formyl-6-hydroxy-2-naphthyl di-sodium phosphate
  参考文献：
  名称：

  Selective Irreversible Inhibition of Fructose 1,6-Bisphosphate Aldolase from Trypanosoma brucei

  摘要：

  An irreversible competitive inhibitor hydroxynaphthaldehyde phosphate was synthesized that is highly selective against the glycolytic enzyme fructose 1,6-bisphosphate aldolase from Trypanosoma brucei (causative agent of sleeping sickness). Inhibition involves Schiff base formation by the inhibitor aldehyde with Lys 116 followed by reaction of the resultant Schiff base with a second residue. Molecular simulations indicate significantly greater molecular geometries conducive for nucleophilic attack in T. brucei aldolase than the mammalian isozyme and suggest Ser48 as the Schiff base modifying residue.

  DOI：

  10.1021/jm050237b
• 作为产物：
  描述：

  1-((phenylimino)methyl)naphthalene-2,6-diol 在 吡啶 、 硫酸 、 碘 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 96.0h， 生成 diethyl (5-formyl-6-hydroxy-2-naphthyl)phosphate
  参考文献：
  名称：

  Selective Irreversible Inhibition of Fructose 1,6-Bisphosphate Aldolase from Trypanosoma brucei

  摘要：

  An irreversible competitive inhibitor hydroxynaphthaldehyde phosphate was synthesized that is highly selective against the glycolytic enzyme fructose 1,6-bisphosphate aldolase from Trypanosoma brucei (causative agent of sleeping sickness). Inhibition involves Schiff base formation by the inhibitor aldehyde with Lys 116 followed by reaction of the resultant Schiff base with a second residue. Molecular simulations indicate significantly greater molecular geometries conducive for nucleophilic attack in T. brucei aldolase than the mammalian isozyme and suggest Ser48 as the Schiff base modifying residue.

  DOI：

  10.1021/jm050237b

文献信息

• Selective Irreversible Inhibition of Fructose 1,6-Bisphosphate Aldolase from <i>Trypanosoma b</i><i>rucei</i>
  作者：Chantal Dax、Francis Duffieux、Nicolas Chabot、Mathieu Coincon、Jurgen Sygusch、Paul A. M. Michels、Casimir Blonski

  DOI：10.1021/jm050237b

  日期：2006.3.1

  An irreversible competitive inhibitor hydroxynaphthaldehyde phosphate was synthesized that is highly selective against the glycolytic enzyme fructose 1,6-bisphosphate aldolase from Trypanosoma brucei (causative agent of sleeping sickness). Inhibition involves Schiff base formation by the inhibitor aldehyde with Lys 116 followed by reaction of the resultant Schiff base with a second residue. Molecular simulations indicate significantly greater molecular geometries conducive for nucleophilic attack in T. brucei aldolase than the mammalian isozyme and suggest Ser48 as the Schiff base modifying residue.