thiophosphoric acid O-isopropyl ester-O',O''-bis-(4-nitro-phenyl ester) | 423771-31-7

• 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: thiophosphoric acid O-isopropyl ester-O',O''-bis-(4-nitro-phenyl ester)
• 英文别名: Thiophosphorsaeure-O-isopropylester-O',O''-bis-(4-nitro-phenylester)；Bis(4-nitrophenoxy)-propan-2-yloxy-sulfidophosphanium；bis(4-nitrophenoxy)-propan-2-yloxy-sulfidophosphanium
• CAS: 423771-31-7
• 化学式: C₁₅H₁₅N₂O₇PS
• 分子量: 398.333
• InChiKey: PISSQXKSUIADEC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.7
• 重原子数：
  26
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  120
• 氢给体数：
  0
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  thiophosphoric acid O-isopropyl ester-O',O''-bis-(4-nitro-phenyl ester) 在 enzyme H₂₅₄G 、 2-环己胺基乙磺酸 作用下， 以 1,4-二氧六环 为溶剂， 生成 (S)-Thiophosphoric acid O-isopropyl ester O'-(4-nitro-phenyl) ester
  参考文献：
  名称：

  Enzymatic Synthesis of Chiral Organophosphothioates from Prochiral Precursors

  摘要：

  The phosphotriesterase from Pseudomonas diminuta has been shown to selectively cleave the pro-R p-nitrophenolate substituent from bis-p-nitrophenyl alkyl phosphothioate esters. When the alkyl substituent is methyl, ethyl, or isopropyl the enantiomeric excess of the product is >/=99%. Manipulation of the active site through mutagenesis has enabled the preparation of protein variants that preferentially hydrolyze the pro-S substituent of the target substrates. This methodology thus permits the preparation of chiral products from prochiral precursors.

  DOI：

  10.1021/ja017840d
• 作为产物：
  描述：

  O,O,O-三(4-硝基苯基)硫代磷酸酯 、 异丙醇 在 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 生成 thiophosphoric acid O-isopropyl ester-O',O''-bis-(4-nitro-phenyl ester)
  参考文献：
  名称：

  Enzymatic Synthesis of Chiral Organophosphothioates from Prochiral Precursors

  摘要：

  The phosphotriesterase from Pseudomonas diminuta has been shown to selectively cleave the pro-R p-nitrophenolate substituent from bis-p-nitrophenyl alkyl phosphothioate esters. When the alkyl substituent is methyl, ethyl, or isopropyl the enantiomeric excess of the product is >/=99%. Manipulation of the active site through mutagenesis has enabled the preparation of protein variants that preferentially hydrolyze the pro-S substituent of the target substrates. This methodology thus permits the preparation of chiral products from prochiral precursors.

  DOI：

  10.1021/ja017840d

文献信息

• Enzymatic Synthesis of Chiral Organophosphothioates from Prochiral Precursors
  作者：Wen-Shan Li、Yingchun Li、Craig M. Hill、Karin T. Lum、Frank M. Raushel

  DOI：10.1021/ja017840d

  日期：2002.4.1

  The phosphotriesterase from Pseudomonas diminuta has been shown to selectively cleave the pro-R p-nitrophenolate substituent from bis-p-nitrophenyl alkyl phosphothioate esters. When the alkyl substituent is methyl, ethyl, or isopropyl the enantiomeric excess of the product is >/=99%. Manipulation of the active site through mutagenesis has enabled the preparation of protein variants that preferentially hydrolyze the pro-S substituent of the target substrates. This methodology thus permits the preparation of chiral products from prochiral precursors.