N^α-pentenoyl-phospho(1-(2-nitrophenyl)ethyl)-L-tyrosine cyanomethyl ester

• 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: N^α-pentenoyl-phospho(1-(2-nitrophenyl)ethyl)-L-tyrosine cyanomethyl ester
• 英文别名: [4-[(2S)-3-(cyanomethoxy)-3-oxo-2-(pent-4-enoylamino)propyl]phenoxy]-[1-(2-nitrophenyl)ethoxy]phosphinic acid
• 化学式: C₂₄H₂₆N₃O₉P
• 分子量: 531.459
• InChiKey: IVAZRXZEDJTGFE-LFABVHOISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  37
• 可旋转键数：
  14
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  187
• 氢给体数：
  2
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  L-酪氨酸叔丁酯 在 四氮唑 、 氢氧化钾 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 为溶剂， 反应 2.5h， 生成 N^α-pentenoyl-phospho(1-(2-nitrophenyl)ethyl)-L-tyrosine cyanomethyl ester
  参考文献：
  名称：

  Caged Phosphoproteins

  摘要：

  We present the chemical and biological synthesis of caged phosphoproteins using the in vitro nonsense codon suppression methodology. Specifically, phosphoamino acid analogues of serine, threonine, and tyrosine with a single photocleavable o-nitrophenylethyl caging group were synthesized as the amino acyl tRNA adducts for insertion into full-length proteins. For this purpose, a novel phosphitylating agent was developed. The successful incorporation of these bulky and charged amino acids into the alpha-subunit of the nicotinic acetyl choline receptor (nAChR) and the vasodilator-stimulated phosphoprotein (VASP) using an in vitro translation system is reported.

  DOI：

  10.1021/ja043875c

文献信息

• Caged Phosphoproteins
  作者：Deborah M. Rothman、E. James Petersson、M. Eugenio Vázquez、Gabriel S. Brandt、Dennis A. Dougherty、Barbara Imperiali

  DOI：10.1021/ja043875c

  日期：2005.1.1

  We present the chemical and biological synthesis of caged phosphoproteins using the in vitro nonsense codon suppression methodology. Specifically, phosphoamino acid analogues of serine, threonine, and tyrosine with a single photocleavable o-nitrophenylethyl caging group were synthesized as the amino acyl tRNA adducts for insertion into full-length proteins. For this purpose, a novel phosphitylating agent was developed. The successful incorporation of these bulky and charged amino acids into the alpha-subunit of the nicotinic acetyl choline receptor (nAChR) and the vasodilator-stimulated phosphoprotein (VASP) using an in vitro translation system is reported.