| 193223-08-4

• 分子结构分类: 有机化合物 - 有机氧化合物
• CAS: 193223-08-4
• 化学式: C₂₉H₅₀O₈Si₂
• 分子量: 582.882
• InChiKey: LPQPGSGSRZEAKI-HDHXAKMKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.37
• 重原子数：
  39.0
• 可旋转键数：
  12.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.69
• 拓扑面积：
  92.68
• 氢给体数：
  1.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  在 ammonium cerium(IV) nitrate 、 氨 、 N,N'-羰基二咪唑 作用下， 以 水 、 乙腈 为溶剂， 反应 8.0h， 生成 (2S,3R,4S,5R,6R)-6-Allyloxy-4,5-bis-(tert-butyl-dimethyl-silanyloxy)-3-hydroxy-tetrahydro-pyran-2-carboxylic acid amide
  参考文献：
  名称：

  A Moenomycin-type Structural Analogue of Lipid II some possible mechanisms of the mode of action of transglycosylase inhibitors can be discarded

  摘要：

  The transglycosylation step in the peptidoglycan biosynthesis belongs to the general class of glycosyltransferase-catalyzed reactions. The structural analogue 2 of moenomycin A has been synthesized and has been found to be antibiotically inactive. The assumption that moenomycin-type transglycosylase inhibitors such as 1 bind at the donor site of the enzyme and that their mode of action is the result of the high stability of the sugar --> phosphate bond seems to be ruled out by the present results.

  DOI：

  10.1002/prac.19973390162
• 作为产物：
  描述：

  Acetic acid (2R,3R,4S,5R,6R)-3,5-diacetoxy-2-acetoxymethyl-6-allyloxy-tetrahydro-pyran-4-yl ester 在 咪唑 、 2,2,6,6-tetramethyl-piperidine-N-oxyl 、 sodium hypochlorite 、 三甲基氯硅烷 、 四丁基氯化铵 、 sodium methylate 、 sodium cyanoborohydride 、 碳酸氢钠 、 对甲苯磺酸 、 sodium chloride 、 potassium bromide 作用下， 以 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 20.0~40.0 ℃ 、10.0 kPa 条件下， 反应 109.0h， 生成
  参考文献：
  名称：

  A Moenomycin-type Structural Analogue of Lipid II some possible mechanisms of the mode of action of transglycosylase inhibitors can be discarded

  摘要：

  The transglycosylation step in the peptidoglycan biosynthesis belongs to the general class of glycosyltransferase-catalyzed reactions. The structural analogue 2 of moenomycin A has been synthesized and has been found to be antibiotically inactive. The assumption that moenomycin-type transglycosylase inhibitors such as 1 bind at the donor site of the enzyme and that their mode of action is the result of the high stability of the sugar --> phosphate bond seems to be ruled out by the present results.

  DOI：

  10.1002/prac.19973390162