(3R,4R)-3-acetoxy-1-benzyloxycarbonyl-4-hydroxypiperidine | 886847-37-6

• 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: (3R,4R)-3-acetoxy-1-benzyloxycarbonyl-4-hydroxypiperidine
• 英文别名: benzyl (3R,4R)-3-acetyloxy-4-hydroxypiperidine-1-carboxylate
• CAS: 886847-37-6
• 化学式: C₁₅H₁₉NO₅
• 分子量: 293.32
• InChiKey: LCCOPCICJUPXQB-ZIAGYGMSSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  21
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  76.1
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (3R,4R)-3-acetoxy-1-benzyloxycarbonyl-4-hydroxypiperidine 在 sodium methylate 作用下， 以 甲醇 为溶剂， 生成 (+)-N-benzyloxycarbonyl-3,4-dihydroxypiperidine
  参考文献：
  名称：

  Biocatalytic preparation of enantioenriched 3,4-dihydroxypiperidines and theoretical study of Candida antarctica lipase B enantioselectivity

  摘要：

  Enzymatic acetylations of N-substituted cis- and trans-3,4-dihydroxypiperidine and hydrolysis of their diacetylated derivatives have been studied. High enantioselectivities are obtained with Pseudomonas cepacia lipase and Candida antarctica lipase B for the hydrolysis of the trans-derivative, while the cis-derivatives are not adequate substrates in the same biocatalytic conditions. The enantiopreference of these processes can be rationalized by means of a molecular modelling study. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2006.01.061
• 作为产物：
  描述：

  N-苯甲氧基甲酰基-1,2,5,6-四氢吡啶 在 Candida antarctica lipase B 、 三氟化硼乙醚 、 水 、 溶剂黄146 、 间氯过氧苯甲酸 作用下， 以 二氯甲烷 、 乙腈 为溶剂， 反应 32.0h， 生成 (3R,4R)-3-acetoxy-1-benzyloxycarbonyl-4-hydroxypiperidine
  参考文献：
  名称：

  Biocatalytic preparation of enantioenriched 3,4-dihydroxypiperidines and theoretical study of Candida antarctica lipase B enantioselectivity

  摘要：

  Enzymatic acetylations of N-substituted cis- and trans-3,4-dihydroxypiperidine and hydrolysis of their diacetylated derivatives have been studied. High enantioselectivities are obtained with Pseudomonas cepacia lipase and Candida antarctica lipase B for the hydrolysis of the trans-derivative, while the cis-derivatives are not adequate substrates in the same biocatalytic conditions. The enantiopreference of these processes can be rationalized by means of a molecular modelling study. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2006.01.061