N-Allyloxycarbonyl-L-serine(O-diallylphosphate) | 175729-26-7

• 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-Allyloxycarbonyl-L-serine(O-diallylphosphate)
• 英文别名: N-Allyloxycarbonyl-O-diallylphosphato-L-serine；(2S)-3-bis(prop-2-enoxy)phosphoryloxy-2-(prop-2-enoxycarbonylamino)propanoic acid
• CAS: 175729-26-7
• 化学式: C₁₃H₂₀NO₈P
• 分子量: 349.277
• InChiKey: HOKSFJVVNQJVJV-NSHDSACASA-N

物化性质

• 沸点：
  484.9±45.0 °C(Predicted)
• 密度：
  1.252±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  23
• 可旋转键数：
  14
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  120
• 氢给体数：
  2
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  N-Allyloxycarbonyl-L-serine(O-diallylphosphate) 在 N-羟基-7-氮杂苯并三氮唑 、 phosphate buffer 、 三正丁胺 、 butyrylcholine esterase (30 U) 、 达卡巴嗪 作用下， 反应 78.5h， 生成 N-Allyloxycarbonyl-L-seryl(O-diallylphosphato)-L-alanine
  参考文献：
  名称：

  Chemoenzymatic Synthesis of Nucleopeptides

  摘要：

  Nucleoproteins, in which the hydroxy group of a serine, a threonine, or a tyrosine, is linked through a phosphodiester group to the 3'- or 5'-end of DNA or RNA, play decisive roles in important biological processes. They may even have a major part in the process of viral replication by nucleoprotein-primed elongation of the oligonucleotide strand. For the study of the biological phenomena, in which nucleoproteins are involved, nucleopeptides with the characteristic linkage between the peptide chain and the oligonucleotide of their parent nucleoproteins may serve as powerful tools. However, the synthesis of these compounds is complicated by their pronounced acid- and base-lability, as well as their multifunctionality. As a result, protecting groups, which can be removed under the mildest conditions, are required. For the construction of such peptide conjugates using a flexible building block strategy, a combination of enzyme-labile and chemical protecting groups was developed. The C-terminal blocking function can be removed selectively from fully protected nucleoamino acid methyl, 2-methoxyethyl (ME), and methoxyethoxyethyl (MEE) esters by saponification of the esters. After elongation of the peptide chain with amino acid or peptide methyl, ME, MEE, and choline esters, the C-terminal ester blocking group can again be removed easily. The methyl, ME, and MEE esters are cleaved off with lipase, and the choline ester group is selectively attacked by butyrylcholine esterase. The nucleoamino acids and peptides formed may be fully deprotected. To this end, the enzyme-labile N-phenylacetyl (PhAc) group, which was employed to mask the amino functions of the nucleobases, was removed. The O-acetate in the deoxyribose was saponified, and the allyl protecting groups present were cleaved by Pd-0-mediated allyl transfer. By combination of these techniques, a nucleopeptide was produced, which represents the characteristic linkage region of the nucleoprotein of adenovions 2. The conditions, under which the enzymatic deprotections proceed, are so mild that no undesired side reaction is observed, that is no depurination or beta elimination of the nucleosides occurs. In addition, the specificity of the biocatalysts ensures that the peptide bonds and the other protecting groups present are not attacked either.

  DOI：

  10.1002/(sici)1521-3765(19990201)5:2<669::aid-chem669>3.0.co;2-v
• 作为产物：
  描述：

  甲基N-[(烯丙氧基)羰基]-L-丝氨酸酯 在 四氮唑 、 phosphate buffer 、 L-半胱氨酸 、 间氯过氧苯甲酸 、 papain 作用下， 以 二氯甲烷 、 丙酮 为溶剂， 反应 0.5h， 生成 N-Allyloxycarbonyl-L-serine(O-diallylphosphate)
  参考文献：
  名称：

  Chemoenzymatic Synthesis of Nucleopeptides

  摘要：

  Nucleoproteins, in which the hydroxy group of a serine, a threonine, or a tyrosine, is linked through a phosphodiester group to the 3'- or 5'-end of DNA or RNA, play decisive roles in important biological processes. They may even have a major part in the process of viral replication by nucleoprotein-primed elongation of the oligonucleotide strand. For the study of the biological phenomena, in which nucleoproteins are involved, nucleopeptides with the characteristic linkage between the peptide chain and the oligonucleotide of their parent nucleoproteins may serve as powerful tools. However, the synthesis of these compounds is complicated by their pronounced acid- and base-lability, as well as their multifunctionality. As a result, protecting groups, which can be removed under the mildest conditions, are required. For the construction of such peptide conjugates using a flexible building block strategy, a combination of enzyme-labile and chemical protecting groups was developed. The C-terminal blocking function can be removed selectively from fully protected nucleoamino acid methyl, 2-methoxyethyl (ME), and methoxyethoxyethyl (MEE) esters by saponification of the esters. After elongation of the peptide chain with amino acid or peptide methyl, ME, MEE, and choline esters, the C-terminal ester blocking group can again be removed easily. The methyl, ME, and MEE esters are cleaved off with lipase, and the choline ester group is selectively attacked by butyrylcholine esterase. The nucleoamino acids and peptides formed may be fully deprotected. To this end, the enzyme-labile N-phenylacetyl (PhAc) group, which was employed to mask the amino functions of the nucleobases, was removed. The O-acetate in the deoxyribose was saponified, and the allyl protecting groups present were cleaved by Pd-0-mediated allyl transfer. By combination of these techniques, a nucleopeptide was produced, which represents the characteristic linkage region of the nucleoprotein of adenovions 2. The conditions, under which the enzymatic deprotections proceed, are so mild that no undesired side reaction is observed, that is no depurination or beta elimination of the nucleosides occurs. In addition, the specificity of the biocatalysts ensures that the peptide bonds and the other protecting groups present are not attacked either.

  DOI：

  10.1002/(sici)1521-3765(19990201)5:2<669::aid-chem669>3.0.co;2-v

文献信息

• Selective Enzymatic Removal of Protecting Groups from Phosphopeptides: Chemoenzymatic Synthesis of a Characteristic Phosphopeptide Fragment of the Raf-1 Kinase
  作者：Dagmar Sebastian

  DOI：10.1055/s-1997-1306

  日期：1997.9

  Base-labile biologically relevant phosphopeptides can advantageously be synthesized under very mild conditions and without undesired side reactions by employing the heptyl (Hep) ester as C-terminal or the phenylacetamide (PhAc) as N-terminal enzyme-labile protecting group. The lipase-mediated saponification of the heptyl ester blocking function was successfully applied in the construction of a characteristic selectively phosphorylated hydroxyamino acid fragment of Raf-1 kinase, an important member of the so-called Ras signal transduction pathway.

  通过采用庚酯(Hep)作为C-末端或苯乙酰胺(PhAc)作为N-末端酶不稳定保护基团，可以有利地在非常温和的条件下合成碱不稳定的生物学相关磷酸肽，并且没有不希望的副反应。脂肪酶介导的庚酯阻断功能皂化已成功应用于构建 Raf-1 激酶的特征性选择性磷酸化羟基氨基酸片段，Raf-1 激酶是所谓的 Ras 信号转导途径的重要成员。
• Chemoenzymatic Synthesis of a Characteristic Phosphorylated and Glycosylated Peptide Fragment of the Large Subunit of Mammalian RNA Polymerase II
  作者：Torsten Pohl、Herbert Waldmann

  DOI：10.1021/ja970709e

  日期：1997.7.1

  The covalent modification of proteins by phosphorylation and addition of GlcNAc residues are important regulatory processes which mediate biological signal transduction. For instance, the cytosolic form of RNA polymerase II is heavily glycosylated but during its transition from an initiating to an elongating complex the carbohydrates are removed and the protein is phosphorylated. For the study of such biological phenomena, characteristic peptides which embody both types of modifications may serve as efficient tools. However, their synthesis is complicated by their pronounced acid and base lability as well as their multifunctionality. These properties make the application of protecting groups necessary which can be removed under the mildest conditions. For the construction of such peptide conjugates the enzyme labile PhAcOZ urethane blocking group was developed. This protecting group embodies (a) a functional group (a phenylacetate) that is recognized by the biocatalyst (penicillin G acylase) and that is bound by an enzyme labile linkage (an ester) to (b) a functional group (a p-hydroxybenzyl urethane) that undergoes a spontaneous fragmentation upon cleavage of the enzyme-sensitive bond resulting in (c) the liberation of a carbamic acid derivative which decarboxylates to give the desired peptide or peptide conjugate. When this enzymatic protecting group technique was combined with classical chemical methods, a complex phosphoglycohexapeptide was built up, which embodies two glycosylated, one phosphorylated, and one underivatized hydroxyamino acid. This peptide represents a characteristic partial structure of the repeat sequence of the large subunit of RNA polymerase II which becomes glycosylated or phosphorylated while the enzyme carries out its biological functions. The conditions under which the enzymatic deprotections proceed are so mild that no undesired side reaction is observed (i.e., no rupture or anomerization of the glycosidic bonds and no beta-elimination of the phosphate or a carbohydrate occur). In addition, the specificity of the biocatalyst guarantees that the peptide bonds and the other protecting groups present are not attacked either.
• Pohl, Torsten; Waldmann, Herbert, Angewandte Chemie, 1996, vol. 108, # 15, p. 1829 - 1832
  作者：Pohl, Torsten、Waldmann, Herbert

  DOI：——

  日期：——
• Chemoenzymatic Synthesis of a Characteristic Glycophosphopeptide from the Transactivation Domain of the Serum Response Factor
  作者：Jörg Sander、Herbert Waldmann

  DOI：10.1002/(sici)1521-3773(19990503)38:9<1250::aid-anie1250>3.0.co;2-m

  日期：1999.5.3

  Glycopeptides, phosphopeptides, and glycophosphopeptides can be synthesized efficiently by a strategy based on a combination of suitable enzyme-labile protecting groups. Thus, probes for biological studies can be accessed. An example is the glycosylated and phosphorylated heptapeptide 1 from the transactivation domain of the human serum response factor, which contains an additional biotin label for detection with streptavidin.
• Chemoenzymatic Synthesis of a Characteristic Phosphopeptide Fragment of the Raf-1 Kinase
  作者：Dagmar Sebastian、Herbert Waldmann

  DOI：10.1016/s0040-4039(97)00514-5

  日期：1997.4

  Base-labile biologically relevant phosphopeptides can advantageously be synthesized under very mild conditions (pH 7, 37 degrees C) by employing the heptyl (Hep) ester as enzyme-labile protecting group. This method was used in the construction of a characteristic, selectively phosphorylated hydroxyamino acid fragment of the Raf-l kinase, an important constituent of the Ras pathway of signal transduction. (C) 1997 Elsevier Science Ltd.