benzyl (2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1→3)-2-acetamido-4,6-benzylidene-2-deoxy-α-D-galactopyranoside | 86327-84-6

• 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: benzyl (2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1→3)-2-acetamido-4,6-benzylidene-2-deoxy-α-D-galactopyranoside
• 英文别名: benzyl 2-acetamido-4,6-O-benzylidene-2-deoxy-3-O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-α-D-galactopyranoside；[(2R,3S,4S,5R,6R)-6-[[(4aR,6S,7R,8R,8aR)-7-acetamido-2-phenyl-6-phenylmethoxy-4,4a,6,7,8,8a-hexahydropyrano[3,2-d][1,3]dioxin-8-yl]oxy]-3,4,5-triacetyloxyoxan-2-yl]methyl acetate
• CAS: 86327-84-6
• 化学式: C₃₆H₄₃NO₁₅
• 分子量: 729.735
• InChiKey: SFCZXSUFIPUMPQ-IZURHRLQSA-N

物化性质

• 溶解度：
  可溶于氯仿、二氯甲烷、DMSO

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  52
• 可旋转键数：
  16
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  190
• 氢给体数：
  1
• 氢受体数：
  15

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-benzylidene-2-deoxy-α-D-galactopyranoside 在 吡啶 、 4-二甲氨基吡啶 、 盐酸羟胺 、 氢气 、 sodium acetate 、 palladium(II) hydroxide 、 溶剂黄146 作用下， 以 甲醇 、 水 为溶剂， 生成 2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl-(1→3)-2-acetamido-4,5-di-O-acetyl-2-deoxy-D-galactose oxime
  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
• 作为产物：
  描述：

  苯甲醇 在 mercury(II) cyanide 、 乙酰氯 、 zinc(II) chloride 作用下， 以 硝基甲烷 、 苯 为溶剂， 生成 benzyl (2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-(1→3)-2-acetamido-4,6-benzylidene-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

文献信息

• A practical synthesis of 2-acetamido-2-deoxy-3,4-di-O-β-d-galactopyranosyl-d-galactopyranose
  作者：Surjit S. Rana、Khushi L. Matta

  DOI：10.1016/s0008-6215(00)90954-6

  日期：1983.5