<(diethoxyphosphoryl)methyl(ethoxy)phosphoryl>methyl 2,3,4,5,6-pentafluorobenzenesulfonate | 240432-44-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: <(diethoxyphosphoryl)methyl(ethoxy)phosphoryl>methyl 2,3,4,5,6-pentafluorobenzenesulfonate
• 英文别名: [Diethoxyphosphorylmethyl(ethoxy)phosphoryl]methyl 2,3,4,5,6-pentafluorobenzenesulfonate
• CAS: 240432-44-4
• 化学式: C₁₄H₁₉F₅O₈P₂S
• 分子量: 504.306
• InChiKey: LLSHMYOQYGFWOJ-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  30
• 可旋转键数：
  12
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  114
• 氢给体数：
  0
• 氢受体数：
  13

反应信息

• 作为反应物：
  描述：

  <(diethoxyphosphoryl)methyl(ethoxy)phosphoryl>methyl 2,3,4,5,6-pentafluorobenzenesulfonate 在 palladium on activated charcoal sodium azide 、 氢气 作用下， 以 乙醇 为溶剂， 25.0 ℃ 、101.33 kPa 条件下， 反应 41.0h， 生成 ethyl aminomethyl<(diethoxyphosphoryl)methyl>phosphinate
  参考文献：
  名称：

  α-Functionalized Phosphonylphosphinates:  Synthesis and Evaluation as Transcarbamoylase Inhibitors

  摘要：

  Diverse alpha-methyl-substituted phosphonylphosphinates (P-C-P-C-X) are accessible from a protected, pentafluorophenylsulfonated phosphonylphosphinate via nucleophilic displacement. The utility of this route is demonstrated with several nitrogen nucleophiles. The resulting amine and amino acid phosphonylphosphinate derivatives were evaluated as inhibitors of Streptococcus faecalis ornithine transcarbamoylase (OTC). Compared with the structurally related phosphonoacetyl-L-ornithine (L-PALO), a known inhibitor of OTCs from various sources, the phosphonylphosphinates are surprisingly poor inhibitors, binding several orders of magnitude less tightly to the enzyme. These results suggest that the tetrahedral intermediate formed in the normal transcarbamoylase reaction is poorly mimicked by a tetrahedral and anionic phosphonate, either because of directly unfavorable interactions with a hydrogen-bond acceptor within the active site or because transition-state analogues are unable to induce the protein conformation changes that normally accompany reaction.

  DOI：

  10.1021/jm991008q
• 作为产物：
  描述：

  ethyl benzyloxymethyl<(diethoxyphosphoryl)methyl>phosphinate 在 palladium on activated charcoal 、 水 氢气 、 N,N-二异丙基乙胺 作用下， 以 乙醇 、 二氯甲烷 为溶剂， -78.0~-15.0 ℃ 、101.33 kPa 条件下， 反应 27.0h， 生成 <(diethoxyphosphoryl)methyl(ethoxy)phosphoryl>methyl 2,3,4,5,6-pentafluorobenzenesulfonate
  参考文献：
  名称：

  α-Functionalized Phosphonylphosphinates:  Synthesis and Evaluation as Transcarbamoylase Inhibitors

  摘要：

  Diverse alpha-methyl-substituted phosphonylphosphinates (P-C-P-C-X) are accessible from a protected, pentafluorophenylsulfonated phosphonylphosphinate via nucleophilic displacement. The utility of this route is demonstrated with several nitrogen nucleophiles. The resulting amine and amino acid phosphonylphosphinate derivatives were evaluated as inhibitors of Streptococcus faecalis ornithine transcarbamoylase (OTC). Compared with the structurally related phosphonoacetyl-L-ornithine (L-PALO), a known inhibitor of OTCs from various sources, the phosphonylphosphinates are surprisingly poor inhibitors, binding several orders of magnitude less tightly to the enzyme. These results suggest that the tetrahedral intermediate formed in the normal transcarbamoylase reaction is poorly mimicked by a tetrahedral and anionic phosphonate, either because of directly unfavorable interactions with a hydrogen-bond acceptor within the active site or because transition-state analogues are unable to induce the protein conformation changes that normally accompany reaction.

  DOI：

  10.1021/jm991008q

文献信息

• α-Functionalized Phosphonylphosphinates:  Synthesis and Evaluation as Transcarbamoylase Inhibitors
  作者：Alexander Flohr、Andreas Aemissegger、Donald Hilvert

  DOI：10.1021/jm991008q

  日期：1999.7.1

  Diverse alpha-methyl-substituted phosphonylphosphinates (P-C-P-C-X) are accessible from a protected, pentafluorophenylsulfonated phosphonylphosphinate via nucleophilic displacement. The utility of this route is demonstrated with several nitrogen nucleophiles. The resulting amine and amino acid phosphonylphosphinate derivatives were evaluated as inhibitors of Streptococcus faecalis ornithine transcarbamoylase (OTC). Compared with the structurally related phosphonoacetyl-L-ornithine (L-PALO), a known inhibitor of OTCs from various sources, the phosphonylphosphinates are surprisingly poor inhibitors, binding several orders of magnitude less tightly to the enzyme. These results suggest that the tetrahedral intermediate formed in the normal transcarbamoylase reaction is poorly mimicked by a tetrahedral and anionic phosphonate, either because of directly unfavorable interactions with a hydrogen-bond acceptor within the active site or because transition-state analogues are unable to induce the protein conformation changes that normally accompany reaction.