(2S,3R)-3-hydroxy-2-[[(2S)-1-[[4-(2-phenylacetyl)oxyphenyl]methoxycarbonyl]pyrrolidine-2-carbonyl]amino]butanoic acid | 182485-50-3

• 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: (2S,3R)-3-hydroxy-2-[[(2S)-1-[[4-(2-phenylacetyl)oxyphenyl]methoxycarbonyl]pyrrolidine-2-carbonyl]amino]butanoic acid
• CAS: 182485-50-3
• 化学式: C₂₅H₂₈N₂O₈
• 分子量: 484.506
• InChiKey: VBZFVWTWVNDCLQ-BUVFEPMLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  35
• 可旋转键数：
  11
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  143
• 氢给体数：
  3
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  (2S,3R)-3-hydroxy-2-[[(2S)-1-[[4-(2-phenylacetyl)oxyphenyl]methoxycarbonyl]pyrrolidine-2-carbonyl]amino]butanoic acid 、 tert-butyl (2S)-3-[(2R,3R,4R,5S,6R)-3-acetamido-4,5-diacetyloxy-6-(acetyloxymethyl)oxan-2-yl]oxy-2-[[(2S)-1-[(2S)-3-[(2R,3R,4R,5S,6R)-3-acetamido-4,5-diacetyloxy-6-(acetyloxymethyl)oxan-2-yl]oxy-2-aminopropanoyl]pyrrolidine-2-carbonyl]amino]propanoate 在 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 作用下， 以71%的产率得到N-[4-(phenylacetoxy)benzyloxycarbonyl]-L-prolyl-L-threonyl-O-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-L-seryl-L-prolyl-O-(2'-acetamido-3',4',6'-tri-O-acetyl-2'-deoxy-β-D-glucopyranosyl)-L-serine, tert-butyl ester
  参考文献：
  名称：

  Pohl, Torsten; Waldmann, Herbert, Angewandte Chemie, 1996, vol. 108, # 15, p. 1829 - 1832

  摘要：

  DOI：
• 作为产物：
  描述：

  PhAcOZ-Pro-OH 在 吗啉 、 四(三苯基膦)钯 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 2.5h， 生成 (2S,3R)-3-hydroxy-2-[[(2S)-1-[[4-(2-phenylacetyl)oxyphenyl]methoxycarbonyl]pyrrolidine-2-carbonyl]amino]butanoic acid
  参考文献：
  名称：

  Chemoenzymatic Synthesis of a Characteristic Phosphorylated and Glycosylated Peptide Fragment of the Large Subunit of Mammalian RNA Polymerase II

  摘要：

  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.

  DOI：

  10.1021/ja970709e

文献信息

• 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 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.