苄基2-O-(苄基磺酰基)-alpha-D-阿拉伯糖吡喃糖苷 | 61134-28-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 中文名称: 苄基2-O-(苄基磺酰基)-alpha-D-阿拉伯糖吡喃糖苷
• 英文名称: benzyl 2-O-p-tosyl-α-D-arabinopyranoside
• 英文别名: Benzyl-2-O-toluolsulfonyl-alpha-D-arabinopyranoside；[(2S,3S,4R,5R)-4,5-dihydroxy-2-phenylmethoxyoxan-3-yl] 4-methylbenzenesulfonate
• CAS: 61134-28-9
• 化学式: C₁₉H₂₂O₇S
• 分子量: 394.445
• InChiKey: BCCUYJAJLVFEBJ-YRXWBPOGSA-N

物化性质

• 沸点：
  592.3±50.0 °C(Predicted)
• 密度：
  1.40±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  27
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.37
• 拓扑面积：
  111
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  苄基2-O-(苄基磺酰基)-alpha-D-阿拉伯糖吡喃糖苷 在 甲醇 、 sodium 作用下， 以72%的产率得到苄基 2,3-脱水-alpha-D-核吡喃糖苷
  参考文献：
  名称：

  Synthesis and inhibition properties of a series of pyranose derivatives towards a Zn-metalloproteinase from Saccharomonospora canescens

  摘要：

  The Zn-proteinase, isolated from Saccharomonospora canescens (NPS), shares many common features with thermolysin, but considerable differences are also evident, as far as the substrate recognition site is concerned. In substrates of general structure AcylAlaAlaPhe 4NA, this neutral proteinase cleaves only the arylamide bond (non-typical activity of Zn-proteinases), while thermolysin attacks the peptide bond Ala-Phe. Phosphoramidon is a powerful tight binding inhibitor for thermolysin and significantly less specific towards NPS. The K-i-values (65 mu M for NPS vs 0.034 mu M for thermolysin) differ nearly 2000-folds. This implies significant differences in the specificity of the corresponding subsites. The carbohydrate moiety is supposed to accommodate in the S-1-subsite and the series of arabinopyranosides and glucopyranosides (12 compounds), which are assayed as inhibitors in a model system: NPS with SucAlaAlaPhe4NA as a substrate could be considered as mapping the S-1-subsite of NPS. Members of the series with an additional ring (3,4-epithio, 3,4-anhydro-derivatives) turned out to be reasonably good competitive inhibitors (K-i approximate to 0.1-0.2 mM are of the same order as the value for phosphoramidon). The structure of these compounds (8, 9, 11 and 12) seems to fit the size of the S-1-subsite and due to an appropriately oriented OH-group in addition, to protect the active site Zn2+. (C) 2010 Published by Elsevier Ltd.

  DOI：

  10.1016/j.carres.2010.07.038
• 作为产物：
  描述：

  D-阿拉伯糖 在 吡啶 、 氢溴酸 、 sodium methylate 、 对甲苯磺酸 、 溶剂黄146 作用下， 以 甲醇 、 二氯甲烷 、 丙酮 为溶剂， 生成 苄基2-O-(苄基磺酰基)-alpha-D-阿拉伯糖吡喃糖苷
  参考文献：
  名称：

  Khan, Noshena; Al-Abed, Yousef; Kohlbau, Hans-Juergen, Zeitschrift fur Naturforschung, B: Chemical Sciences, 1996, vol. 51, # 12, p. 1781 - 1790

  摘要：

  DOI：

文献信息

• Khan, Noshena; Al-Abed, Yousef; Kohlbau, Hans-Juergen, Zeitschrift fur Naturforschung, B: Chemical Sciences, 1996, vol. 51, # 12, p. 1781 - 1790
  作者：Khan, Noshena、Al-Abed, Yousef、Kohlbau, Hans-Juergen、Latif-Ansari, Farzana、Kowollik, Wolfgang、Voelter, Wolfgang

  DOI：——

  日期：——
• Synthesis and inhibition properties of a series of pyranose derivatives towards a Zn-metalloproteinase from Saccharomonospora canescens
  作者：Pavlina Dolashka-Angelova、Raid J. Abdel-Jalil、Raed A. Al-Qawasmeh、Nicolina Stambolieva、Wolfgang Voelter

  DOI：10.1016/j.carres.2010.07.038

  日期：2010.11

  The Zn-proteinase, isolated from Saccharomonospora canescens (NPS), shares many common features with thermolysin, but considerable differences are also evident, as far as the substrate recognition site is concerned. In substrates of general structure AcylAlaAlaPhe 4NA, this neutral proteinase cleaves only the arylamide bond (non-typical activity of Zn-proteinases), while thermolysin attacks the peptide bond Ala-Phe. Phosphoramidon is a powerful tight binding inhibitor for thermolysin and significantly less specific towards NPS. The K-i-values (65 mu M for NPS vs 0.034 mu M for thermolysin) differ nearly 2000-folds. This implies significant differences in the specificity of the corresponding subsites. The carbohydrate moiety is supposed to accommodate in the S-1-subsite and the series of arabinopyranosides and glucopyranosides (12 compounds), which are assayed as inhibitors in a model system: NPS with SucAlaAlaPhe4NA as a substrate could be considered as mapping the S-1-subsite of NPS. Members of the series with an additional ring (3,4-epithio, 3,4-anhydro-derivatives) turned out to be reasonably good competitive inhibitors (K-i approximate to 0.1-0.2 mM are of the same order as the value for phosphoramidon). The structure of these compounds (8, 9, 11 and 12) seems to fit the size of the S-1-subsite and due to an appropriately oriented OH-group in addition, to protect the active site Zn2+. (C) 2010 Published by Elsevier Ltd.