Boc-L-Phe-OCH2CN | 127357-85-1

• 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: Boc-L-Phe-OCH2CN
• 英文别名: (S)-cyanomethyl 2-(tert-butoxycarbonylamino)-3-phenylpropanoate；Boc-Phe-OCH2CN；cyanomethyl (2S)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-3-phenylpropanoate
• CAS: 127357-85-1
• 化学式: C₁₆H₂₀N₂O₄
• 分子量: 304.346
• InChiKey: HORGGQWLSZFGMZ-ZDUSSCGKSA-N

物化性质

• 沸点：
  485.4±40.0 °C(Predicted)
• 密度：
  1.153±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.1
• 重原子数：
  22
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  88.4
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  Boc-L-Phe-OCH2CN 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 12.0h， 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
• 作为产物：
  描述：

  BOC-L-苯丙氨酸 、 氯乙腈 在 三乙胺 作用下， 反应 2.0h， 以89%的产率得到Boc-L-Phe-OCH2CN
  参考文献：
  名称：

  酶作为合成催化剂：天然和改性胰凝乳蛋白酶的机理和活性位点考虑

  摘要：

  本文描述了{α}-胰凝乳蛋白酶和（Met{sub 192}-亚砜）-{α}-胰凝乳蛋白酶在动力学控制过程（即氨解）中催化的肽合成的机理研究以及两种酶在不同的条件。确定了与水竞争酰基酶中间体的各种亲核试剂（包括 D-和 L-氨基酸）的分配参数。这些参数提供了对天然酶和氧化酶的活性位点几何形状的深入了解。在{α}-甲基-{α}-硝基酯的水解中具有D-异构体选择性的{α}-糜蛋白酶用于合成DL假肽。分子模型与动力学结果一起用于解释由天然酶和修饰酶催化的水解和合成中的异常现象。在活性位点组氨酸的 {epsilon}{sub 2}-N 处甲基化的 {α}-胰凝乳蛋白酶被证明是动力学控制过程中肽合成的有效催化剂。没有观察到肽键水解。

  DOI：

  10.1021/ja00169a043

文献信息

• Methods of modifying N-termini of a peptide or protein using transferases
  申请人：The Trustees of the University of Pennsylvania

  公开号：US09376700B2

  公开（公告）日：2016-06-28

  The invention includes a selective method of modifying the N-terminus of a protein using an aminoacyl tRNA transferase. In certain embodiments, the method comprises contacting a solution of the protein or peptide with a transferase and a derivative of a molecule, whereby the N-terminus of the protein or peptide is derivatized with the molecule.

  该发明涉及使用氨酰基tRNA转移酶选择性地修改蛋白质的N-末端的方法。在某些实施例中，该方法包括将蛋白质或肽溶液与转移酶和分子衍生物接触，从而使蛋白质或肽的N-末端与该分子衍生物发生衍生化反应。
• 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.
• Enzymes as synthetic catalysts: mechanistic and active-site considerations of natural and modified chymotrypsin
  作者：J. Blair West、William J. Hennen、James L. Lalonde、Jeffrey A. Bibbs、Ziyang Zhong、Edgar F. Meyer、Chi Huey Wong

  DOI：10.1021/ja00169a043

  日期：1990.6

  into the active-site geometries of both the native and the oxidized enzymes. alpha}-Chymotrypsin with D-isomer selectivity in the hydrolysis of alpha}-methyl-alpha}-nitro esters was used for the synthesis of a D-L pseudopeptide. Molecular modeling together with kinetic results was used to explain the unusual phenomena in hydrolysis and synthesis catalyzed by the native and modified enzymes. alpha}-Chymotrypsin

  本文描述了α}-胰凝乳蛋白酶和（Metsub 192}-亚砜）-α}-胰凝乳蛋白酶在动力学控制过程（即氨解）中催化的肽合成的机理研究以及两种酶在不同的条件。确定了与水竞争酰基酶中间体的各种亲核试剂（包括 D-和 L-氨基酸）的分配参数。这些参数提供了对天然酶和氧化酶的活性位点几何形状的深入了解。在α}-甲基-α}-硝基酯的水解中具有D-异构体选择性的α}-糜蛋白酶用于合成DL假肽。分子模型与动力学结果一起用于解释由天然酶和修饰酶催化的水解和合成中的异常现象。在活性位点组氨酸的 epsilon}sub 2}-N 处甲基化的 α}-胰凝乳蛋白酶被证明是动力学控制过程中肽合成的有效催化剂。没有观察到肽键水解。