2-acetamino-2-deoxy-3-O-(phenoxythiocarbonyl)-1,3,6-tri-O-acetyl-α-D-glucopyranose | 1190619-65-8

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-acetamino-2-deoxy-3-O-(phenoxythiocarbonyl)-1,3,6-tri-O-acetyl-α-D-glucopyranose
• CAS: 1190619-65-8
• 化学式: C₂₁H₂₅NO₁₀S
• 分子量: 483.496
• InChiKey: VQKVXEOEFRQPHK-WAPOTWQKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.02
• 重原子数：
  33.0
• 可旋转键数：
  7.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.48
• 拓扑面积：
  135.69
• 氢给体数：
  1.0
• 氢受体数：
  11.0

反应信息

• 作为反应物：
  描述：

  2-acetamino-2-deoxy-3-O-(phenoxythiocarbonyl)-1,3,6-tri-O-acetyl-α-D-glucopyranose 在 甲醇 、 偶氮二异丁腈 、 3,5-二硝基水杨酸 、 三正丁基氢锡 、 sodium methylate 作用下， 反应 0.25h， 生成
  参考文献：
  名称：

  Substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4 towards galactose, glucose, and their derivatives

  摘要：

  Galactokinases (GalKs) have attracted significant research attention for their potential applications in the enzymatic synthesis of unique sugar phosphates. The galactokinase (GalKSpe4) cloned from Streptococcus pneumoniae TIGR4 presents a remarkably broad substrate range including 14 diverse natural and unnatural sugars. TLC and MS studies revealed that GalKSpe4 had relaxed activity towards galactose derivatives with modifications on the C-6, 4- or 2-positions. Additionally, GalKSpe4 can also tolerate glucose while glucose derivatives with modifications on the C-6, 4- or 2-positions were unacceptable. More interestingly, GalKSpe4 can phosphorylate L-mannose in moderate yield (43%), while other L-sugars such as L-Gal cannot be recognized by this enzyme. These results are very significant because there is rarely enzyme reported that can phosphorylate such uncommon substrates as L-mannose. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2012.03.095
• 作为产物：
  描述：

  phenyl chlorothionocarbonate 、 (+)-2-acetamido-1,3,6-tri-O-acetyl-2-deoxy-α-D-glucopyranoside 在 4-二甲氨基吡啶 作用下， 生成 2-acetamino-2-deoxy-3-O-(phenoxythiocarbonyl)-1,3,6-tri-O-acetyl-α-D-glucopyranose
  参考文献：
  名称：

  Substrate specificity of galactokinase from Streptococcus pneumoniae TIGR4 towards galactose, glucose, and their derivatives

  摘要：

  Galactokinases (GalKs) have attracted significant research attention for their potential applications in the enzymatic synthesis of unique sugar phosphates. The galactokinase (GalKSpe4) cloned from Streptococcus pneumoniae TIGR4 presents a remarkably broad substrate range including 14 diverse natural and unnatural sugars. TLC and MS studies revealed that GalKSpe4 had relaxed activity towards galactose derivatives with modifications on the C-6, 4- or 2-positions. Additionally, GalKSpe4 can also tolerate glucose while glucose derivatives with modifications on the C-6, 4- or 2-positions were unacceptable. More interestingly, GalKSpe4 can phosphorylate L-mannose in moderate yield (43%), while other L-sugars such as L-Gal cannot be recognized by this enzyme. These results are very significant because there is rarely enzyme reported that can phosphorylate such uncommon substrates as L-mannose. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2012.03.095

文献信息

• Substrate specificity of N-acetylhexosamine kinase towards N-acetylgalactosamine derivatives
  作者：Li Cai、Wanyi Guan、Wenjun Wang、Wei Zhao、Motomitsu Kitaoka、Jie Shen、Crystal O’Neil、Peng George Wang

  DOI：10.1016/j.bmcl.2009.07.104

  日期：2009.9

  We report herein a bacterial N-acetylhexosamine kinase, NahK, with broad substrate specificity towards structurally modified GalNAc analogues, and the production of a GalNAc-1-phosphate library using this kinase.

  我们在这里报告细菌N-乙酰己糖胺激酶，NahK，对结构修饰的GalNAc类似物具有广泛的底物特异性，并使用该激酶生产GalNAc-1-磷酸文库。