N-(4-Phenylacetoxybenzyloxycarbonyl)-L-serine(O-2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl) | 182485-44-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: N-(4-Phenylacetoxybenzyloxycarbonyl)-L-serine(O-2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)
• 英文别名: (2S)-3-[(2R,3R,4R,5S,6R)-3-acetamido-4,5-diacetyloxy-6-(acetyloxymethyl)oxan-2-yl]oxy-2-[[4-(2-phenylacetyl)oxyphenyl]methoxycarbonylamino]propanoic acid
• CAS: 182485-44-5
• 化学式: C₃₃H₃₈N₂O₁₅
• 分子量: 702.669
• InChiKey: KUIOIBYGTGCPRL-BQEMODBLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  50
• 可旋转键数：
  20
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  228
• 氢给体数：
  3
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  N-(4-Phenylacetoxybenzyloxycarbonyl)-L-serine(O-2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl) 在 四(三苯基膦)钯 吗啉 、 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， 生成 (S)-1-[(S)-3-((2R,3R,4R,5S,6R)-4,5-Diacetoxy-6-acetoxymethyl-3-acetylamino-tetrahydro-pyran-2-yloxy)-2-(4-phenylacetoxy-benzyloxycarbonylamino)-propionyl]-pyrrolidine-2-carboxylic acid
  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：

  A-D-氨基葡萄糖五乙酸盐 在 4 A molecular sieve 、 三氟化硼乙醚 、 三乙胺 作用下， 以 二氯甲烷 、 乙腈 为溶剂， 反应 24.07h， 生成 N-(4-Phenylacetoxybenzyloxycarbonyl)-L-serine(O-2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)
  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

• Enzymatic Protecting Group Techniques for Glyco- and Phosphopeptide Chemistry: Synthesis of a Glycophosphopeptide from Human Serum Response Factor
  作者：Jörg Sander、Herbert Waldmann

  DOI：10.1002/(sici)1521-3765(20000502)6:9<1564::aid-chem1564>3.3.co;2-h

  日期：2000.5.2

  The covalent modification of proteins by phosphorylation and by glycosylation with GlcNAc residues are important regulatory processes which mediate biological signal transduction. For the study of such biological phenomena in molecular detail characteristic peptides which embody both types of modification may serve as efficient tools. However, their synthesis is complicated by their pronounced acid and base lability as well as their multifunctionality. For this purpose the enzyme labile choline ester was developed. The choline ester can be removed selectively and in high yields from various GlcNAc-glycopeptides and phosphopeptides at pH 6.5 and 37 degrees C. The conditions under which the enzymatic deprotections proceed are so mild that no undesirable side reactions are observed (i.e., no cleavage or anomerization of the glycosidic bonds and no beta-elimination of the phosphate or the carbohydrate occur). The specificity of the biocatalyst guarantees that neither the peptide bonds nor the other protecting groups present are being attacked. When this enzymatic protecting group technique was combined with the enzyme-labile 4-(phenylacetoxy)benzyloxycarbonyl (PhAcOZ) urethane protecting group a complex glycophosphopeptide could be built up. The glycopeptide is equipped with a biotin label by which it can be traced in biological systems. This peptide represents a characteristic partial structure of a glycosylated and phosphorylated sequence from the transactivation domain of serum response factor (SRF), a widely occuring human transcription factor.
• 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.