(2R,3R)-4-benzyloxy-3-methyl-2,3-epoxybutanyl methanesulfonate | 1196056-91-3

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: (2R,3R)-4-benzyloxy-3-methyl-2,3-epoxybutanyl methanesulfonate
• CAS: 1196056-91-3
• 化学式: C₁₃H₁₈O₅S
• 分子量: 286.349
• InChiKey: JYFNPGDRIPIMRO-CHWSQXEVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.34
• 重原子数：
  19.0
• 可旋转键数：
  7.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.54
• 拓扑面积：
  65.13
• 氢给体数：
  0.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  (2R,3R)-4-benzyloxy-3-methyl-2,3-epoxybutanyl methanesulfonate 在 甲酸 、 1% Pd/C 作用下， 以 甲醇 为溶剂， 以76%的产率得到(2R,3R)-4-hydroxy-3-methyl-2,3-epoxybutanyl methanesulfonate
  参考文献：
  名称：

  IspG Converts an Epoxide Substrate Analogue to (E)-4-Hydroxy-3-methylbut-2-enyl Diphosphate: Implications for IspG Catalysis in Isoprenoid Biosynthesis

  摘要：

  IspG is an intriguing enzyme in bacteria, parasite, and plant isoprenoid biosynthesis, and its catalytic mechanism remains elusive. We report here the synthesis of (2R,3R)-4-hydroxy-3-methyl-2,3-epoxybutanyl diphosphate (Epoxy-HMBPP), a proposed intermediate in one of the frequently cited mechanistic models. We have also demonstrated that this epoxide analogue is a catalytically competent IspG substrate. This study represents the first mechanistic study of this important enzyme.

  DOI：

  10.1021/ja907470n
• 作为产物：
  描述：

  甲基磺酰氯 、 (2S,3R)-(3-benzyloxymethyl-3-methyl-oxiranyl)-methanol 在 三乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 0.5h， 以98%的产率得到(2R,3R)-4-benzyloxy-3-methyl-2,3-epoxybutanyl methanesulfonate
  参考文献：
  名称：

  IspG Converts an Epoxide Substrate Analogue to (E)-4-Hydroxy-3-methylbut-2-enyl Diphosphate: Implications for IspG Catalysis in Isoprenoid Biosynthesis

  摘要：

  IspG is an intriguing enzyme in bacteria, parasite, and plant isoprenoid biosynthesis, and its catalytic mechanism remains elusive. We report here the synthesis of (2R,3R)-4-hydroxy-3-methyl-2,3-epoxybutanyl diphosphate (Epoxy-HMBPP), a proposed intermediate in one of the frequently cited mechanistic models. We have also demonstrated that this epoxide analogue is a catalytically competent IspG substrate. This study represents the first mechanistic study of this important enzyme.

  DOI：

  10.1021/ja907470n