(2S,3R)-2-amino-3-hydroxy-3-(2-methoxyphenyl)propanoic acid | 1332506-53-2

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (2S,3R)-2-amino-3-hydroxy-3-(2-methoxyphenyl)propanoic acid
• CAS: 1332506-53-2
• 化学式: C₁₀H₁₃NO₄
• 分子量: 211.218
• InChiKey: YMOXGPJHSKTSCA-DTWKUNHWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.5
• 重原子数：
  15
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  92.8
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  邻甲氧基苯甲醛 、 聚甘氨酸 在 recombinant L-threonine aldolases from Escherichia coli 、 磷酸吡哆醛 作用下， 反应 18.0h， 生成 (2S,3S)-2-amino-3-hydroxy-3-(2-methoxyphenyl)propanoic acid 、 (2S,3R)-2-amino-3-hydroxy-3-(2-methoxyphenyl)propanoic acid
  参考文献：
  名称：

  A study towards efficient l-threonine aldolase-catalyzed enantio- and diastereoselective aldol reactions of glycine with substituted benzaldehydes: biocatalyst production and process development

  摘要：

  The development of aldol reactions of glycine with substituted benzaldehydes in the presence of recombinant L-threonine aldolases from Escherichia coli or Saccharomyces cerevisiae, which were obtained with excellent overexpression data, has been carried out. When using glycine and ortho-chlorobenzaldehyde, a high conversion of >95%, an enantioselectivity of >99% ee, and a diastereoselectivity with d.r.(syn/anti) = 80:20 was obtained for the resulting beta-hydroxy alpha-amino acid in such a biotransformation. It should be noted that this enzymatic process can be conducted at an elevated substrate concentration of 250 mM. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2011.04.016

文献信息

• A study towards efficient l-threonine aldolase-catalyzed enantio- and diastereoselective aldol reactions of glycine with substituted benzaldehydes: biocatalyst production and process development
  作者：Katrin Baer、Nina Dückers、Thorsten Rosenbaum、Christian Leggewie、Sabine Simon、Marina Kraußer、Steffen Oßwald、Werner Hummel、Harald Gröger

  DOI：10.1016/j.tetasy.2011.04.016

  日期：2011.5

  The development of aldol reactions of glycine with substituted benzaldehydes in the presence of recombinant L-threonine aldolases from Escherichia coli or Saccharomyces cerevisiae, which were obtained with excellent overexpression data, has been carried out. When using glycine and ortho-chlorobenzaldehyde, a high conversion of >95%, an enantioselectivity of >99% ee, and a diastereoselectivity with d.r.(syn/anti) = 80:20 was obtained for the resulting beta-hydroxy alpha-amino acid in such a biotransformation. It should be noted that this enzymatic process can be conducted at an elevated substrate concentration of 250 mM. (C) 2011 Elsevier Ltd. All rights reserved.