2-hydroxy-2-(1-methyl-2-pyrrolyl)acetonitrile

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡咯
• 英文名称: 2-hydroxy-2-(1-methyl-2-pyrrolyl)acetonitrile
• 英文别名: 2-Hydroxy-2-(1-methylpyrrol-2-yl)acetonitrile；2-hydroxy-2-(1-methylpyrrol-2-yl)acetonitrile
• 化学式: C₇H₈N₂O
• 分子量: 136.153
• InChiKey: XNXMFKDJDLFWNX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  10
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  49
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  叔丁基二甲基氯硅烷 、 2-hydroxy-2-(1-methyl-2-pyrrolyl)acetonitrile 在 咪唑 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 tert-butyldimethylsilyloxy(1-methyl-2-pyrrolyl)acetonitrile
  参考文献：
  名称：

  Asymmetric biocatalytic hydrocyanation of pyrrole carboxaldehydes

  摘要：

  The asymmetric hydrocyanation of pyrrole-2- and -3-carboxaldehydes substituted with either methyl, benzyl or phenyl in the I-position catalyzed by the hydroxynitrile lyases from Hevea brasiliensis (HbHNL) and Prunus amygdalus (PaHNL) is reported. The products could be isolated-after O-sitylation-with moderate to good enantiomeric purity although the carbon, I activity of the substrates was found to be very low, which is supported by quantum-chemical calculations. Structural effects concerning substrate size and regiochemistry are discussed considering docking calculations based on the X-ray crystal structures of the two enzymes. From these calculations one particular amino acid residue (Trp-128) in the active site of HbHNL could be identified, which plays a major role for the appropriate binding of structurally demanding carbonyl compounds. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2005.05.095
• 作为产物：
  描述：

  N-甲基-2-吡咯甲醛 、 氢氰酸 在 Amberlyst-A₂₁ 作用下， 以 various solvent(s) 为溶剂， 生成 2-hydroxy-2-(1-methyl-2-pyrrolyl)acetonitrile
  参考文献：
  名称：

  Asymmetric biocatalytic hydrocyanation of pyrrole carboxaldehydes

  摘要：

  The asymmetric hydrocyanation of pyrrole-2- and -3-carboxaldehydes substituted with either methyl, benzyl or phenyl in the I-position catalyzed by the hydroxynitrile lyases from Hevea brasiliensis (HbHNL) and Prunus amygdalus (PaHNL) is reported. The products could be isolated-after O-sitylation-with moderate to good enantiomeric purity although the carbon, I activity of the substrates was found to be very low, which is supported by quantum-chemical calculations. Structural effects concerning substrate size and regiochemistry are discussed considering docking calculations based on the X-ray crystal structures of the two enzymes. From these calculations one particular amino acid residue (Trp-128) in the active site of HbHNL could be identified, which plays a major role for the appropriate binding of structurally demanding carbonyl compounds. (c) 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2005.05.095

文献信息

• A study of asymmetric hydrocyanation of heteroaryl carboxaldehydes catalyzed by (R)-oxynitrilase under micro-aqueous conditions
  作者：Peiran Chen、Shiqing Han、Guoqiang Lin、Hao Huang、Zuyi Li

  DOI：10.1016/s0957-4166(02)00005-8

  日期：2001.12

  A number of new optically active heteroaryl cyanohydrins have been prepared by hydrocyanation under micro-aqueous conditions catalyzed by almond meal (containing (R)-oxynitrilase). Substituent effects on the reaction are discussed. This micro-aqueous method provides an efficient, convenient and economical approach to optically active cyanohydrins. (C) 2002 Published by Elsevier Science Ltd.
• Asymmetric biocatalytic hydrocyanation of pyrrole carboxaldehydes
  作者：Thomas Purkarthofer、Karl Gruber、Martin H. Fechter、Herfried Griengl

  DOI：10.1016/j.tet.2005.05.095

  日期：2005.8

  The asymmetric hydrocyanation of pyrrole-2- and -3-carboxaldehydes substituted with either methyl, benzyl or phenyl in the I-position catalyzed by the hydroxynitrile lyases from Hevea brasiliensis (HbHNL) and Prunus amygdalus (PaHNL) is reported. The products could be isolated-after O-sitylation-with moderate to good enantiomeric purity although the carbon, I activity of the substrates was found to be very low, which is supported by quantum-chemical calculations. Structural effects concerning substrate size and regiochemistry are discussed considering docking calculations based on the X-ray crystal structures of the two enzymes. From these calculations one particular amino acid residue (Trp-128) in the active site of HbHNL could be identified, which plays a major role for the appropriate binding of structurally demanding carbonyl compounds. (c) 2005 Elsevier Ltd. All rights reserved.