Z-Asnβ-(Ac3GlcNAc)LeuThrNH2 | 129835-75-2

• 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: Z-Asnβ-(Ac3GlcNAc)LeuThrNH2
• 英文别名: [(2R,3S,4R,5R,6R)-5-acetamido-3,4-diacetyloxy-6-[[(3S)-4-[[(2S)-1-[[(2S,3R)-1-amino-3-hydroxy-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-oxo-3-(phenylmethoxycarbonylamino)butanoyl]amino]oxan-2-yl]methyl acetate
• CAS: 129835-75-2
• 化学式: C₃₆H₅₂N₆O₁₅
• 分子量: 808.84
• InChiKey: RNEBWXYYFAIPQJ-RNFAIECXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.1
• 重原子数：
  57
• 可旋转键数：
  23
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  306
• 氢给体数：
  7
• 氢受体数：
  15

反应信息

• 作为反应物：
  描述：

  Z-Asnβ-(Ac3GlcNAc)LeuThrNH2 在 palladium on activated charcoal 水 、 氢气 、 溶剂黄146 作用下， 以 甲醇 为溶剂， 反应 15.0h， 以79%的产率得到2-acetamido-3,4,6-tri-O-acetyl-1-N-<(aspartylleucylthreoninamid)-4.1-yl>-2-deoxy-β-D-glucopyranosylamine
  参考文献：
  名称：

  Yeast oligosaccharyltransferase: glycosylation of peptide substrates and chemical characterization of the glycopeptide product

  摘要：

  The product of the reaction catalyzed by yeast oligosaccharyltransferase was examined in order to determine the nature of the chemical linkage between the sugar and peptide. Biosynthetic donor lipid [H-3]oligosaccharide was prepared and used as a substrate for yeast oligosaccharyltransferase together with a chemically synthesized peptide acceptor, N-benzoyl-Asn-Leu-Thr-NH2. the glycosylated peptide product of the in vitro reaction was isolated and hydrolyzed with endo-beta-N-acetylglucosaminidase-H to yield a large oligosaccharide and the glycotripeptide, N-benzoyl-Asn(GlcNAc)-Leu-Thr-Nh2. This glycopeptide was purified using gel filtration, affinity binding, and reverse-phase high-performance liquid chromatography. The biosynthetic glycopeptide was compared with chemically synthesized glycopeptides in which a 1-amino-GlcNAc moiety was linked to either the alpha- or beta-carboxyl of aspartate. It was determined that the sole biosynthetic product has the structure in which the carbohydrate is linked to the peptide through the beta-carbonyl of asparagine, i.e., a normal alpha-peptide. These experiments provide an unambiguous structural proof of the protein-carbohydrate linkage in the glycoprotein product of the oligosaccharyltransferase-catalyzed reaction.

  DOI：

  10.1021/jo00313a013
• 作为产物：
  描述：

  2-乙酰氨基-3,4,6-三-O-乙酰基-2-脱氧-Β-D-吡喃葡萄糖酰基叠氮化物 在 ammonium hydroxide 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 、 三苯基膦 、 三氟乙酸 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 31.5h， 生成 Z-Asnβ-(Ac3GlcNAc)LeuThrNH2
  参考文献：
  名称：

  Yeast oligosaccharyltransferase: glycosylation of peptide substrates and chemical characterization of the glycopeptide product

  摘要：

  The product of the reaction catalyzed by yeast oligosaccharyltransferase was examined in order to determine the nature of the chemical linkage between the sugar and peptide. Biosynthetic donor lipid [H-3]oligosaccharide was prepared and used as a substrate for yeast oligosaccharyltransferase together with a chemically synthesized peptide acceptor, N-benzoyl-Asn-Leu-Thr-NH2. the glycosylated peptide product of the in vitro reaction was isolated and hydrolyzed with endo-beta-N-acetylglucosaminidase-H to yield a large oligosaccharide and the glycotripeptide, N-benzoyl-Asn(GlcNAc)-Leu-Thr-Nh2. This glycopeptide was purified using gel filtration, affinity binding, and reverse-phase high-performance liquid chromatography. The biosynthetic glycopeptide was compared with chemically synthesized glycopeptides in which a 1-amino-GlcNAc moiety was linked to either the alpha- or beta-carboxyl of aspartate. It was determined that the sole biosynthetic product has the structure in which the carbohydrate is linked to the peptide through the beta-carbonyl of asparagine, i.e., a normal alpha-peptide. These experiments provide an unambiguous structural proof of the protein-carbohydrate linkage in the glycoprotein product of the oligosaccharyltransferase-catalyzed reaction.

  DOI：

  10.1021/jo00313a013