methyl (2S)-2-[methyl-(2-oxochromen-7-yl)oxycarbonylamino]-3-phosphonooxypropanoate | 1154580-34-3

• 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-(2-oxochromen-7-yl)oxycarbonylamino]-3-phosphonooxypropanoate
• CAS: 1154580-34-3
• 化学式: C₁₅H₁₆NO₁₀P
• 分子量: 401.266
• InChiKey: UICRPCHNGCPQJZ-NSHDSACASA-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：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  149
• 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-(2-oxochromen-7-yl)oxycarbonylamino]-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 7-羟基香豆素 、 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120 mg的产率得到methyl (2S)-2-[methyl-(2-oxochromen-7-yl)oxycarbonylamino]-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

• Kinetic delay of cyclization/elimination-coupled enzyme assays: Analysis and solution
  作者：Fengtian Xue、Christopher T. Seto

  DOI：10.1016/j.bmcl.2010.09.104

  日期：2011.2

  A kinetic analysis of an enzyme assay employing a synthetic substrate that produces a detectable signal through a spontaneous organic cyclization/elimination reaction following the enzymatic reaction was conducted. The results from the calculation were used to predict the lag period and provide accurate measurements of the activity of alkaline phosphatase using the fluorogenic substrate ( 1). (C) 2010 Published by Elsevier Ltd.