β-benzyl N-(diethoxyphosphinoyl)acetyl-L-isoasparaginate | 913094-94-7

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: β-benzyl N-(diethoxyphosphinoyl)acetyl-L-isoasparaginate
• 英文别名: benzyl (3S)-4-amino-3-[(2-diethoxyphosphorylacetyl)amino]-4-oxobutanoate
• CAS: 913094-94-7
• 化学式: C₁₇H₂₅N₂O₇P
• 分子量: 400.368
• InChiKey: UTTSWWCATWMWGU-AWEZNQCLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  27
• 可旋转键数：
  13
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  134
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  β-benzyl N-(diethoxyphosphinoyl)acetyl-L-isoasparaginate 在 三甲基溴硅烷 、 水 作用下， 以 乙腈 为溶剂， 反应 1.0h， 以100%的产率得到β-benzyl N-phosphonoacetyl-L-isoasparaginate
  参考文献：
  名称：

  N-Phosphonacetyl-l-isoasparagine a Potent and Specific Inhibitor of Escherichia coli Aspartate Transcarbamoylase

  摘要：

  The synthesis of a new inhibitor, N-phosphonacetyl-L-isoasparagine (PALI), of Escherichia coli aspartate transcarbamoylase (ATCase) is reported, as well as structural studies of the enzyme.PALI complex. PALI was synthesized in 7 steps from beta-benzyl L-aspartate. The KD of PALI was 2 microM. Kinetics and small-angle X-ray scattering experiments showed that PALI can induce the cooperative transition of ATCase from the T to the R state. The X-ray structure of the enzyme.PALI complex showed 22 hydrogen-bonding interactions between the enzyme and PALI. The kinetic characterization and crystal structure of the ATCase.PALI complex also provides detailed information regarding the importance of the alpha-carboxylate for the binding of the substrate aspartate.

  DOI：

  10.1021/jm0607294
• 作为产物：
  描述：

  Boc-L-天冬氨酸 4-苄酯 在 吡啶 、 氯甲酸乙酯 、 三乙胺 、 三氟乙酸 作用下， 以 1,4-二氧六环 、 二氯甲烷 为溶剂， 反应 20.5h， 生成 β-benzyl N-(diethoxyphosphinoyl)acetyl-L-isoasparaginate
  参考文献：
  名称：

  N-Phosphonacetyl-l-isoasparagine a Potent and Specific Inhibitor of Escherichia coli Aspartate Transcarbamoylase

  摘要：

  The synthesis of a new inhibitor, N-phosphonacetyl-L-isoasparagine (PALI), of Escherichia coli aspartate transcarbamoylase (ATCase) is reported, as well as structural studies of the enzyme.PALI complex. PALI was synthesized in 7 steps from beta-benzyl L-aspartate. The KD of PALI was 2 microM. Kinetics and small-angle X-ray scattering experiments showed that PALI can induce the cooperative transition of ATCase from the T to the R state. The X-ray structure of the enzyme.PALI complex showed 22 hydrogen-bonding interactions between the enzyme and PALI. The kinetic characterization and crystal structure of the ATCase.PALI complex also provides detailed information regarding the importance of the alpha-carboxylate for the binding of the substrate aspartate.

  DOI：

  10.1021/jm0607294

文献信息

• <i>N</i>-Phosphonacetyl-<scp>l</scp>-isoasparagine a Potent and Specific Inhibitor of <i>Escherichia </i><i>c</i><i>oli</i> Aspartate Transcarbamoylase
  作者：Joby Eldo、James P. Cardia、Elizabeth M. O'Day、Jiarong Xia、Hiro Tsuruta、Evan R. Kantrowitz

  DOI：10.1021/jm0607294

  日期：2006.10.1

  The synthesis of a new inhibitor, N-phosphonacetyl-L-isoasparagine (PALI), of Escherichia coli aspartate transcarbamoylase (ATCase) is reported, as well as structural studies of the enzyme.PALI complex. PALI was synthesized in 7 steps from beta-benzyl L-aspartate. The KD of PALI was 2 microM. Kinetics and small-angle X-ray scattering experiments showed that PALI can induce the cooperative transition of ATCase from the T to the R state. The X-ray structure of the enzyme.PALI complex showed 22 hydrogen-bonding interactions between the enzyme and PALI. The kinetic characterization and crystal structure of the ATCase.PALI complex also provides detailed information regarding the importance of the alpha-carboxylate for the binding of the substrate aspartate.