(2R,3R)-methyl 3-hydroxy-2-iodo-3-(4-methoxyphenyl)-propanoate | 800368-85-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: (2R,3R)-methyl 3-hydroxy-2-iodo-3-(4-methoxyphenyl)-propanoate
• 英文别名: methyl (2R,3R)-3-hydroxy-2-iodo-3-(4-methoxyphenyl)propanoate
• CAS: 800368-85-8
• 化学式: C₁₁H₁₃IO₄
• 分子量: 336.126
• InChiKey: FLRBVGWSLHIPCN-NXEZZACHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.6
• 重原子数：
  16
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  55.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (2R,3R)-methyl 3-hydroxy-2-iodo-3-(4-methoxyphenyl)-propanoate 在 1,8-二氮杂双环[5.4.0]十一碳-7-烯 作用下， 以 二氯甲烷 为溶剂， 反应 0.58h， 生成 (2R,3S)-rel-3-(4-甲氧基苯基)-2-环氧乙烷羧酸甲酯
  参考文献：
  名称：

  Chemoenzymatic approach to optically active phenylglycidates: resolution of bromo- and iodohydrins

  摘要：

  Enantiomerically enriched phenylglycidates, precursors of the taxol C-13 phenylisoserine side chain and diltiazem. were prepared by kinetic resolution of anti-2-bromo-3-hydroxy- and anti-3-hydroxy-2-iodophenylpropanoates to provide enantioriched (2R,3R)- and (2S,3S)-halohydrins. The bulkiness and inflexibility of bromo and iodo groups in halohydrins have made them inaccessible to the active site of most of the lipases utilized for the hydrolysis of their acyloxy derivatives. In a set of 22 hydrolases screened herein, including native as well as commercial enzymes, only Aspergillus niger (Lipase AS, AMANO) could catalyze the hydrolysis with high enantioselectivity (E = 176). The resolved halohydrins easily underwent transformation to the corresponding (2S,3R)- and (2R,3S)phenylglycidates. (C) 26 E'lsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2004.08.026
• 作为产物：
  描述：

  (e)-p-甲氧基肉桂酸甲酯 在 4-二甲氨基吡啶 、 phosphate buffer 、 lipase AS Amano 、 sodium hydrogensulfite 、 过碘酸 作用下， 以 二氯甲烷 、 甲苯 、 乙腈 为溶剂， 反应 95.0h， 生成 (2R,3R)-methyl 3-hydroxy-2-iodo-3-(4-methoxyphenyl)-propanoate
  参考文献：
  名称：

  Chemoenzymatic approach to optically active phenylglycidates: resolution of bromo- and iodohydrins

  摘要：

  Enantiomerically enriched phenylglycidates, precursors of the taxol C-13 phenylisoserine side chain and diltiazem. were prepared by kinetic resolution of anti-2-bromo-3-hydroxy- and anti-3-hydroxy-2-iodophenylpropanoates to provide enantioriched (2R,3R)- and (2S,3S)-halohydrins. The bulkiness and inflexibility of bromo and iodo groups in halohydrins have made them inaccessible to the active site of most of the lipases utilized for the hydrolysis of their acyloxy derivatives. In a set of 22 hydrolases screened herein, including native as well as commercial enzymes, only Aspergillus niger (Lipase AS, AMANO) could catalyze the hydrolysis with high enantioselectivity (E = 176). The resolved halohydrins easily underwent transformation to the corresponding (2S,3R)- and (2R,3S)phenylglycidates. (C) 26 E'lsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2004.08.026