methyl (2S)-2-[methyl-(4-nitrophenoxy)carbonylamino]-3-phosphonooxypropanoate | 1154580-37-6

• 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: methyl (2S)-2-[methyl-(4-nitrophenoxy)carbonylamino]-3-phosphonooxypropanoate
• CAS: 1154580-37-6
• 化学式: C₁₂H₁₅N₂O₁₀P
• 分子量: 378.232
• InChiKey: JGEBPVZSCZDYEG-JTQLQIEISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  25
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  168
• 氢给体数：
  2
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  methyl (2S)-2-[methyl-(4-nitrophenoxy)carbonylamino]-3-phosphonooxypropanoate 在 三羟甲基氨基甲烷 、 magnesium chloride 、 alkaline phosphatase 作用下， 以 水 、 二甲基亚砜 为溶剂， 生成 对硝基苯酚 、 methyl (4S)-3-methyl-2-oxo-1,3-oxazolidine-4-carboxylate
  参考文献：
  名称：

  Fluorogenic Peptide Substrates for Serine and Threonine Phosphatases

  摘要：

  A new fluorescent assay for Ser/Thr protein phosphatases has been developed. Hydrolysis of a phosphoSer residue liberates the Ser hydroxyl group, which induces a cyclization reaction on the N-terminal carbamate and releases a fluorescent reporter. Sequence selectivity is observed using several peptide substrates against alkaline phosphatase (ALP), bacteriophage lambda protein phosphatase (lambda-PPase), and vaccinia H1 related phosphatase (VHR). These studies suggest that the assay could be a useful tool for profiling the substrate specificities of medicinally important phosphatases.

  DOI：

  10.1021/ol1003065
• 作为产物：
  描述：

  在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 0.33h， 以163 mg的产率得到methyl (2S)-2-[methyl-(4-nitrophenoxy)carbonylamino]-3-phosphonooxypropanoate
  参考文献：
  名称：

  Fluorogenic Peptide Substrates for Serine and Threonine Phosphatases

  摘要：

  A new fluorescent assay for Ser/Thr protein phosphatases has been developed. Hydrolysis of a phosphoSer residue liberates the Ser hydroxyl group, which induces a cyclization reaction on the N-terminal carbamate and releases a fluorescent reporter. Sequence selectivity is observed using several peptide substrates against alkaline phosphatase (ALP), bacteriophage lambda protein phosphatase (lambda-PPase), and vaccinia H1 related phosphatase (VHR). These studies suggest that the assay could be a useful tool for profiling the substrate specificities of medicinally important phosphatases.

  DOI：

  10.1021/ol1003065

文献信息

• Fluorogenic Peptide Substrates for Serine and Threonine Phosphatases
  作者：Fengtian Xue、Christopher T. Seto

  DOI：10.1021/ol1003065

  日期：2010.5.7

  A new fluorescent assay for Ser/Thr protein phosphatases has been developed. Hydrolysis of a phosphoSer residue liberates the Ser hydroxyl group, which induces a cyclization reaction on the N-terminal carbamate and releases a fluorescent reporter. Sequence selectivity is observed using several peptide substrates against alkaline phosphatase (ALP), bacteriophage lambda protein phosphatase (lambda-PPase), and vaccinia H1 related phosphatase (VHR). These studies suggest that the assay could be a useful tool for profiling the substrate specificities of medicinally important phosphatases.