(S)-(2R,3R,4R,5R)-2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl 2-amino-3-phenylpropanoate | 5956-81-0

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷
• 英文名称: (S)-(2R,3R,4R,5R)-2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl 2-amino-3-phenylpropanoate
• 英文别名: A-Phe；Phe-A；O^3'-phenylalanyl-adenosine；[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] (2S)-2-amino-3-phenylpropanoate
• CAS: 5956-81-0
• 化学式: C₁₉H₂₂N₆O₅
• 分子量: 414.421
• InChiKey: WTCLHPCVOYZEIY-URQYDQELSA-N

物化性质

• 沸点：
  723.8±70.0 °C(Predicted)
• 密度：
  1.67±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.1
• 重原子数：
  30
• 可旋转键数：
  7
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.37
• 拓扑面积：
  172
• 氢给体数：
  4
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  (S)-(2R,3R,4R,5R)-2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl 2-amino-3-phenylpropanoate 、 7-赖氨酰丙氨酰-4-甲基香豆素酰胺 在 His₁₀-tagged E_. coli aminoacyl transferase 作用下， 以 aq. buffer 为溶剂， 反应 4.0h， 以100%的产率得到PheLysAlaAcm
  参考文献：
  名称：

  蛋氨酸处表达蛋白连接：同型半胱氨酸的 N 端连接、连接和掩蔽

  摘要：

  一个有用的句柄：蛋白质半合成的一个主要限制是在天然化学连接反应中需要在连接位点使用 Cys。结果表明，转移酶可以将同型半胱氨酸传递到表达蛋白质的 N 端（参见方案）。同型半胱氨酸可用于连接反应，然后转化为 Met。这允许人们使用 MetArg 或 MetLys 基序作为半合成中的断开点。

  DOI：

  10.1002/anie.201302065
• 作为产物：
  描述：

  BOC-L-苯丙氨酸琥珀酰亚胺酯 在 三异丙基硅烷 、 四丁基醋酸铵 、 三氟乙酸 作用下， 以 四氢呋喃 为溶剂， 反应 60.0h， 生成 (S)-(2R,3R,4R,5R)-2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl 2-amino-3-phenylpropanoate
  参考文献：
  名称：

  N-Terminal Protein Modification Using Simple Aminoacyl Transferase Substrates

  摘要：

  Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.

  DOI：

  10.1021/ja2055098

文献信息

• Biomimetic protecting-group-free 2′, 3′-selective aminoacylation of nucleosides and nucleotides
  作者：Sohyoung Her、Ronald Kluger

  DOI：10.1039/c0ob00795a

  日期：——

  Aminoacyl phosphate monoesters can be prepared free of an amino-protecting group and used directly in lanthanum-promoted selective monoacylation of either the 2′ or 3′-hydroxyl of nucleosides and nucleotides. For example, phenylalanyl ethyl phosphate rapidly forms esters with either of the 2′ or 3′-hydroxyls of ribonucleosides and nucleotides in the presence of lanthanum ions in aqueous buffer. Oligomerization

  可以制备不含氨基保护基的氨基酰基磷酸单酯，并将其直接用于镧促进的核苷和核苷酸的2'或3'-羟基选择性单酰基化。例如，在水缓冲液中存在镧离子的情况下，磷酸苯丙氨酰基乙基磷酸酯与核糖核苷的2'或3'-羟基和核苷酸迅速形成酯。氨酰基磷酸的低聚比酯的形成慢得多，并且不是竞争性的过程。试剂的竞争性水解缓慢。通过扩展，该途径应提供简化的通向tRNA的合成氨基酰化衍生物的一般途径。
• N-Terminal Protein Modification Using Simple Aminoacyl Transferase Substrates
  作者：Anne M. Wagner、Mark W. Fegley、John B. Warner、Christina L. J. Grindley、Nicholas P. Marotta、E. James Petersson

  DOI：10.1021/ja2055098

  日期：2011.9.28

  Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.
• Expressed Protein Ligation at Methionine: N-Terminal Attachment of Homocysteine, Ligation, and Masking
  作者：Tomohiro Tanaka、Anne M. Wagner、John B. Warner、Yanxin J. Wang、E. James Petersson

  DOI：10.1002/anie.201302065

  日期：2013.6.10

  A useful handle: One major limitation of protein semi‐synthesis is the need for Cys at the ligation site in native chemical ligation reactions. It is shown that a transferase enzyme can deliver homocysteine to the N‐terminus of an expressed protein (see scheme). Homocysteine can be used in a ligation reaction and then converted to Met. This allows one to use the MetArg or MetLys motif as a point of

  一个有用的句柄：蛋白质半合成的一个主要限制是在天然化学连接反应中需要在连接位点使用 Cys。结果表明，转移酶可以将同型半胱氨酸传递到表达蛋白质的 N 端（参见方案）。同型半胱氨酸可用于连接反应，然后转化为 Met。这允许人们使用 MetArg 或 MetLys 基序作为半合成中的断开点。