benzyl (2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1→3)-2-acetamido-4,6-di-O-acetyl-2-deoxy-α-D-galactopyranoside | 3809-10-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: benzyl (2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1→3)-2-acetamido-4,6-di-O-acetyl-2-deoxy-α-D-galactopyranoside
• 英文别名: benzyl 2-acetamido-4,6-di-O-acetyl-2-deoxy-3-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-α-D-galactopyranoside；Benzyl-2-acetamido-4,6-di-O-acetyl-3-O-<2,3,4,6-tetra-O-acetyl-D-galaktopyranosyl>-α-D-galaktopyranosid；Benzyl 2-acetamido-4,6-DI-O-acetyl-3-O-(2,3,4,6-tetra-O-acetyl-B-D-galactopyranosyl)-2-deoxy-A-D-galactopyranoside；[(2R,3R,4R,5R,6S)-5-acetamido-3-acetyloxy-6-phenylmethoxy-4-[(2R,3R,4S,5S,6R)-3,4,5-triacetyloxy-6-(acetyloxymethyl)oxan-2-yl]oxyoxan-2-yl]methyl acetate
• CAS: 3809-10-7
• 化学式: C₃₃H₄₃NO₁₇
• 分子量: 725.701
• InChiKey: JRXJPDIFFVHMRH-MUWZFAHCSA-N

物化性质

• 熔点：
  158-160°C
• 溶解度：
  溶于氯仿

计算性质

• 辛醇/水分配系数(LogP)：
  0.2
• 重原子数：
  51
• 可旋转键数：
  20
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.61
• 拓扑面积：
  224
• 氢给体数：
  1
• 氢受体数：
  17

反应信息

• 作为反应物：
  描述：

  benzyl (2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1→3)-2-acetamido-4,6-di-O-acetyl-2-deoxy-α-D-galactopyranoside 在 四氮唑 、 10% palladium hydroxide on charcoal 、 氢气 、 溶剂黄146 作用下， 以 乙醇 、 二氯甲烷 为溶剂， 反应 23.0h， 生成 2-acetamido-4,6-di-O-acetyl-2-deoxy-3-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-α-D-galactopyranosyl phosphate
  参考文献：
  名称：

  P 1-（11-苯氧基十一烷基）-P 2-（2-乙酰氨基-2-脱氧-3-O-α-D-鼠李糖吡喃糖基-α-D-吡喃葡萄糖基）二磷酸酯和P 1-（11-苯氧基十一烷基）-的合成P 2-（2-乙酰氨基-2-脱氧-3-O-β-D-吡喃半乳糖基-α-D-吡喃半乳糖基）二磷酸用于铜绿假单胞菌和大肠杆菌O104中O抗原多糖的生物合成研究

  摘要：

  首次合成了两个新的苯氧基十一烷基二磷酸糖：P1-（11-苯氧基十一烷基）-P2-（2-乙酰氨基-2-脱氧-3-O-α-D-鼠李糖基吡喃糖基-α-D-葡萄糖基吡喃糖基）二磷酸和P1 -（11-苯氧基十一烷基）-P2-（2-乙酰氨基-2-脱氧-3-O-β-D-吡喃并吡喃糖基-α-D-吡喃并吡喃糖基）二磷酸酯，以研究O抗原重复单元的生物合成的第三步铜绿假单胞菌和大肠杆菌O104中的多糖分别。

  DOI：

  10.1016/j.carres.2017.10.016
• 作为产物：
  描述：

  2-乙酰氨基-2-脱氧-D-吡喃半乳糖 在 吡啶 、 4-二甲氨基吡啶 、 sodium acetate 、 mercury(II) cyanide 、 溶剂黄146 、 乙酰氯 、 zinc(II) chloride 作用下， 以 硝基甲烷 、 水 、 苯 为溶剂， 生成 benzyl (2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1→3)-2-acetamido-4,6-di-O-acetyl-2-deoxy-α-D-galactopyranoside
  参考文献：
  名称：

  Structural Analysis of a Family 101 Glycoside Hydrolase in Complex with Carbohydrates Reveals Insights into Its Mechanism

  摘要：

  O-Linked glycosylation is one of the most abundant post-translational modifications of proteins. Within the secretory pathway of higher eukaryotes, the core of these glycans is frequently an N-acetylgalactosamine residue that is alpha-linked to serine or threonine residues. Glycoside hydrolases in family 101 are presently the only known enzymes to be able to hydrolyze this glycosidic linkage. Here we determine the high-resolution structures of the catalytic domain comprising a fragment of GH101 from Streptococcus pneumoniae TIGR4, SpGH101, in the absence of carbohydrate, and in complex with reaction products, inhibitor, and substrate analogues. Upon substrate binding, a tryptophan lid (residues 724-WNW-726) closes on the substrate. The closing of this lid fully engages the substrate in the active site with Asp-764 positioned directly beneath C1 of the sugar residue bound within the -1 subsite, consistent with its proposed role as the catalytic nucleophile. In all of the bound forms of the enzyme, however, the proposed catalytic acid/base residue was found to be too distant from the glycosidic oxygen (> 4.3 angstrom) to serve directly as a general catalytic acid/base residue and thereby facilitate cleavage of the glycosidic bond. These same complexes, however, revealed a structurally conserved water molecule positioned between the catalytic acid/base and the glycosidic oxygen. On the basis of these structural observations we propose a new variation of the retaining glycoside hydrolase mechanism wherein the intervening water molecule enables a Grotthuss proton shuttle between Glu-796 and the glycosidic oxygen, permitting this residue to serve as the general acid/base catalytic residue.

  DOI：

  10.1074/jbc.m115.680470