α-amino-(3'-fluorophenyl-)methanephosphonic acid | 174587-50-9

• 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: α-amino-(3'-fluorophenyl-)methanephosphonic acid
• 英文别名: [amino-(3-fluorophenyl)methyl]phosphonic acid；Amino(3-fluorophenyl)methylphosphonic acid
• CAS: 174587-50-9
• 化学式: C₇H₉FNO₃P
• mdl: MFCD24388561
• 分子量: 205.126
• InChiKey: VRYPTNKNNGXIOV-UHFFFAOYSA-N

物化性质

• 沸点：
  404.2±55.0 °C(Predicted)
• 密度：
  1.536±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -3.1
• 重原子数：
  13
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.142
• 拓扑面积：
  83.6
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  α-amino-(3'-fluorophenyl-)methanephosphonic acid 在 sodium hydroxide 、 penicillin G acylase from E_. coli 、 碳酸氢钠 作用下， 以 丙酮 为溶剂， 反应 24.0h， 生成 [(R)-Amino-(3-fluoro-phenyl)-methyl]-phosphonic acid
  参考文献：
  名称：

  RESOLUTION OF FLUORINATED AMINOMETHANPHOSPHONIC ACIDS CATALYSED BY PENICILLIN G ACYLASE - III

  摘要：

  In this work, we have used penicillin G acylase (EC 3.5.1.11) from E. coli to resolve kinetically four fluorinated aminomethanphosphonic acids: 1: 1-trifluoromethyl-, 2:1-p-fluorophenyl-, 3:1-m-fluorophenyl-, 4: 1-p-trifluoromethylphenyl-1-aminomethanphosphonic acids. This enzyme catalyses enantioselectively the hydrolysis of the N-phenylacetylated derivatives of 1-4, The enantiomeric excesses determined via P-31 NMR spectra of the diastereomeric Pd(II) complexes of 1-4 were high for each compound studied.

  DOI：

  10.1080/10426509708043557
• 作为产物：
  描述：

  [Acetylamino-(3-fluoro-phenyl)-methyl]-phosphonic acid 在 吡啶 、 盐酸 作用下， 以 甲醇 为溶剂， 生成 α-amino-(3'-fluorophenyl-)methanephosphonic acid
  参考文献：
  名称：

  一些氟化α-氨基芳基甲膦酸的制备和表征

  摘要：

  摘要 α-氨基芳基甲烷膦酸已在苯环（4-F、3-F、2-F、3,4-F2、F5、4-CF3、3- CF3、4-CF3O 和 3-CF3O)。这些化合物具有相对较低的水溶性，因此它们的 NMR 光谱（1H、13C、31P 和 19F）是在过量碱存在的 D2O 中记录的。在这些条件下，环取代基似乎对 δH (15–18 ppm) 或苄基 (α-CH) 的 1H 和 13C 参数几乎没有影响，这些参数主要在其他类型的 α 观察到的范围内-氨基芳基甲烷膦酸在碱性条件下（δH，3.8-4.0 ppm，2 J PH 15.3-16.5 Hz；δc 57-58 ppm，1 J PC 128-132 Hz）。对于邻位氟的那些例子（即，2-氟和五氟衍生物）观察到苄基碳原子（δc 50-51 ppm）的场化学位移略高。在快原子轰击质谱中，伪分子离子、MH+ 和离子导致...

  DOI：

  10.1080/10426509608046389

文献信息

• Substituted phosphonic analogues of phenylglycine as inhibitors of phenylalanine ammonia lyase from potatoes
  作者：Weronika Wanat、Michał Talma、Józef Hurek、Małgorzata Pawełczak、Paweł Kafarski

  DOI：10.1016/j.biochi.2018.06.005

  日期：2018.8

  A series of phosphonic acid analogues of phenylglycine variously substituted in phenyl ring have been synthesized and evaluated for their inhibitory activity towards potato l-phenylalanine ammonia lyase. Most of the compounds appeared to act as moderate (micromolar) inhibitors of the enzyme. Analysis of their binding performed using molecular modeling have shown that they might be bound either in active

  已经合成了一系列在苯环上被各种取代的苯基甘氨酸的膦酸类似物，并评估了它们对马铃薯1-苯基丙氨酸氨裂合酶的抑制活性。大多数化合物似乎充当该酶的中度（微摩尔）抑制剂。使用分子模型进行的结合分析表明，它们可能结合在酶的活性位点或非生理位点。后者位于邻近的深位点，靠近底物进入活性位点的进入通道。
• Inhibitors of phenylalanine ammonia-lyase: 1-aminobenzylphosphonic acids substituted in the benzene ring
  作者：Jerzy Zoń、Nikolaus Amrhein、Roman Gancarz

  DOI：10.1016/s0031-9422(01)00425-3

  日期：2002.1

  Dextrorotatory 1-amino-3',4'-dichlorobenzylphosphonic acid was found to be a potent inhibitor of the plant enzyme phenylalanine ammonia-lyase both in vitro and in vivo from among the ring-substituted 1-aminobenzylphosphonic acids and other analogues of phenylglycine. A structure activity relationship analysis of the results obtained permits predictions on the geometry of the pocket of the enzyme and is a basis in the strategy of better inhibitor synthesis. (C) 2002 Published by Elsevier Science Ltd.
• Tailoring the Structure of Aminobisphosphonates To Target Plant P5C Reductase
  作者：Giuseppe Forlani、Andrea Occhipinti、Łukasz Berlicki、Gabriela Dziedzioła、Anna Wieczorek、Paweł Kafarski

  DOI：10.1021/jf800029t

  日期：2008.5.1

  Using the structure of (3,5-dichlorophenyl)aminomethylenebisphosphonic acid as a lead compound, 25 new phosphonates were synthesized and evaluated as possible inhibitors of Arabidopsis thaliana delta(1)-pyrroline-5-carboxylate (P5C) reductase. Derivatives substituted in the phenyl ring retained the inhibitory potential, though to a different extent. On the contrary any variation in the scaffold, i.e., the replacement of the second phosphonate moiety with a hydroxyl or an amino residue, resulted in a significant loss of biological activity. The availability of several structures capable of interfering with the catalytic mechanism in the micromolar to millimolar range allowed a proper structure-activity relationship analysis, leading us to hypothesize about the steric and electronic requirements for maintenance or enhancement of the inhibitory properties. Reversal experiments with suspension cultured cells provided evidence for the occurrence of enzyme inhibition in vivo. Because in higher plants the step catalyzed by P5C reductase is shared by all pathways leading to proline synthesis, these compounds may be exploited for the design of new substances endowed with herbicidal activity.