Phenoxyaethylphosphonsaeure-diaethylester | 15016-79-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: Phenoxyaethylphosphonsaeure-diaethylester
• 英文别名: (2-phenoxy-ethyl)-phosphonic acid diethyl ester；(2-Phenoxy-aethyl)-phosphonsaeure-diaethylester；2-Diethoxyphosphorylethoxybenzene
• CAS: 15016-79-2
• 化学式: C₁₂H₁₉O₄P
• 分子量: 258.254
• InChiKey: OSDIJGVJHBBKDJ-UHFFFAOYSA-N

物化性质

• 沸点：
  185-187 °C(Press: 10 Torr)
• 密度：
  1.11 g/cm3

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  17
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  44.8
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Phenoxyaethylphosphonsaeure-diaethylester 在 盐酸 作用下， 生成 2-苯氧基乙基膦酸
  参考文献：
  名称：

  A nonhydrolyzable analogue of phosphotyrosine, and related aryloxymethano- and aryloxyethano-phosphonic acids as motifs for inhibition of phosphatases

  摘要：

  Nonhydrolyzable analogues of both stereoisomers of phosphotyrosine, and a series of related aryloxy (or thio) methyl and aryloxy (or thio) ethyl phosphonic acids of the general formula RX-(CH2) -PO3H2 (where X = O or S and n = 1 or 2), have been tested as nonhydrolyzable mimetics of phosphatase substrates. These compounds were tested against a panel of phosphatases (two alkaline phosphatases, a protein-tyrosine phosphatase, and two serine/threonine phosphatases) with different active site motifs. The compounds exhibit competitive inhibition toward all enzymes tested, with the best inhibition expressed toward the Ser/Thr phosphatases. The stereoisomers of the phosphotyrosine analogues exhibited an unexpected difference in their inhibitory properties toward the protein-tyrosine phosphatase from Yersinia. The K-i for the D isomer is 33-fold lower than that of the (L) isomer, and is more than an order of magnitude lower than the reported K, of the substrate L-phosphotyrosine. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2004.09.008
• 作为产物：
  描述：

  苯酚 、 alkaline earth salt of/the/ methylsulfuric acid 在 氢氧化钾 、 四丁基溴化铵 作用下， 生成 Phenoxyaethylphosphonsaeure-diaethylester
  参考文献：
  名称：

  A nonhydrolyzable analogue of phosphotyrosine, and related aryloxymethano- and aryloxyethano-phosphonic acids as motifs for inhibition of phosphatases

  摘要：

  Nonhydrolyzable analogues of both stereoisomers of phosphotyrosine, and a series of related aryloxy (or thio) methyl and aryloxy (or thio) ethyl phosphonic acids of the general formula RX-(CH2) -PO3H2 (where X = O or S and n = 1 or 2), have been tested as nonhydrolyzable mimetics of phosphatase substrates. These compounds were tested against a panel of phosphatases (two alkaline phosphatases, a protein-tyrosine phosphatase, and two serine/threonine phosphatases) with different active site motifs. The compounds exhibit competitive inhibition toward all enzymes tested, with the best inhibition expressed toward the Ser/Thr phosphatases. The stereoisomers of the phosphotyrosine analogues exhibited an unexpected difference in their inhibitory properties toward the protein-tyrosine phosphatase from Yersinia. The K-i for the D isomer is 33-fold lower than that of the (L) isomer, and is more than an order of magnitude lower than the reported K, of the substrate L-phosphotyrosine. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2004.09.008

文献信息

• Nitrogen Mustard Derivatives Containing the Phosphonate Group¹
  作者：Fred Kagan、Robert D. Birkenmeyer、Richard E. Strube

  DOI：10.1021/ja01521a029

  日期：1959.6
• Michailowa, Uchenye Zapiski, Kazanskii Gosudarstvennyi Universitet, 1941, vol. 101, # 3, p. Sbornik stud. Rabot. Nr. 2 S. 58
  作者：Michailowa

  DOI：——

  日期：——
• A nonhydrolyzable analogue of phosphotyrosine, and related aryloxymethano- and aryloxyethano-phosphonic acids as motifs for inhibition of phosphatases
  作者：Subashree Iyer、Jarod M. Younker、Przemyslaw G. Czyryca、Alvan C. Hengge

  DOI：10.1016/j.bmcl.2004.09.008

  日期：2004.12

  Nonhydrolyzable analogues of both stereoisomers of phosphotyrosine, and a series of related aryloxy (or thio) methyl and aryloxy (or thio) ethyl phosphonic acids of the general formula RX-(CH2) -PO3H2 (where X = O or S and n = 1 or 2), have been tested as nonhydrolyzable mimetics of phosphatase substrates. These compounds were tested against a panel of phosphatases (two alkaline phosphatases, a protein-tyrosine phosphatase, and two serine/threonine phosphatases) with different active site motifs. The compounds exhibit competitive inhibition toward all enzymes tested, with the best inhibition expressed toward the Ser/Thr phosphatases. The stereoisomers of the phosphotyrosine analogues exhibited an unexpected difference in their inhibitory properties toward the protein-tyrosine phosphatase from Yersinia. The K-i for the D isomer is 33-fold lower than that of the (L) isomer, and is more than an order of magnitude lower than the reported K, of the substrate L-phosphotyrosine. (C) 2004 Elsevier Ltd. All rights reserved.