1-benzoyl-2-methyl-piperidin-4-one | 13729-76-5

• 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: 1-benzoyl-2-methyl-piperidin-4-one
• 英文别名: N-Benzoyl-2-methyl-4-piperidon；1-Benzoyl-2-methylpiperidin-4-one
• CAS: 13729-76-5
• 化学式: C₁₃H₁₅NO₂
• 分子量: 217.268
• InChiKey: QAHSDYAKLVNWDV-UHFFFAOYSA-N

物化性质

• 沸点：
  377.8±35.0 °C(Predicted)
• 密度：
  1.137±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  16
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  37.4
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  (2-methylpiperidin-1-yl)(phenyl)methanone 在 Beauveria Bassiana ATCC 7159 、 氧气 作用下， 生成 1-benzoyl-2-methylpiperidin-3-ol 、 1-benzoyl-2-methylpiperidin-4-ol 、 1-benzoyl-2-methyl-piperidin-4-one
  参考文献：
  名称：

  Biohydroxylation Reactions Catalyzed by Enzymes and Whole-Cell Systems

  摘要：

  The biohydroxylation of a number of cyclic substrates (3-24) containing aromatic side chains was used to compare substrate specificity and selectivity of hydroxylation using microbial enzymes and whole-cell biocatalysts. In general, the regioselectivity of reaction was remarkably similar between the different catalysts in that little aromatic or benzylic, but significant aliphatic hydroxylation was observed. However, a more detailed investigation of isolated products showed complementary substrate specificity, functional group compatibility, and regioselectivity of hydroxylation. Substrate specificity and regioselectivity could be further modulated by small changes to the nature of the aromatic side chain, which appears to play an important role in substrate recognition, (C) 1999 Academic Press.

  DOI：

  10.1006/bioo.1999.1135

文献信息

• Biohydroxylation Reactions Catalyzed by Enzymes and Whole-Cell Systems
  作者：Sabine L. Flitsch、Suzanne J. Aitken、Cathy S.-Y. Chow、Gideon Grogan、Adam Staines

  DOI：10.1006/bioo.1999.1135

  日期：1999.4

  The biohydroxylation of a number of cyclic substrates (3-24) containing aromatic side chains was used to compare substrate specificity and selectivity of hydroxylation using microbial enzymes and whole-cell biocatalysts. In general, the regioselectivity of reaction was remarkably similar between the different catalysts in that little aromatic or benzylic, but significant aliphatic hydroxylation was observed. However, a more detailed investigation of isolated products showed complementary substrate specificity, functional group compatibility, and regioselectivity of hydroxylation. Substrate specificity and regioselectivity could be further modulated by small changes to the nature of the aromatic side chain, which appears to play an important role in substrate recognition, (C) 1999 Academic Press.