(R)-N-phenylacetyl-2-heptylamine

• 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: (R)-N-phenylacetyl-2-heptylamine
• 英文别名: N-[(2R)-heptan-2-yl]-2-phenylacetamide
• 化学式: C₁₅H₂₃NO
• 分子量: 233.354
• InChiKey: AXQPRWQTJNNBAO-CYBMUJFWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  17
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  29.1
• 氢给体数：
  1
• 氢受体数：
  1

反应信息

• 作为产物：
  描述：

  异庚胺 、 苯乙酸甲酯 在 Novozym 435 、 4 A molecular sieve 作用下， 以 异丙醚 为溶剂， 反应 24.0h， 生成 (R)-N-phenylacetyl-2-heptylamine
  参考文献：
  名称：

  Penicillin acylase-catalyzed resolution of amines in aqueous organic solvents

  摘要：

  Penicillin acylase from Alcaligenes faecalis catalyzes the enantioselective acylation of amines with phenylacetamide in a kinetically controlled reaction in water at pH II. Addition of cosolvent to the reaction mixture significantly improved the enantioselectivity in most cases. Penicillin acylase from E. coli also catalyzed the phenylacetylation of amines, but an order of magnitude less efficiently than with the enzyme of A. faecalis. Amine resolution via kinetically controlled acylation competes effectively with hydrolysis of N-acylated compounds and constitutes a synthetically useful alternative to existing lipase-based methods. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(00)00442-0

文献信息

• Penicillin acylase-catalyzed resolution of amines in aqueous organic solvents
  作者：L.M. van Langen、N.H.P. Oosthoek、D.T. Guranda、F. van Rantwijk、V.K. Švedas、R.A. Sheldon

  DOI：10.1016/s0957-4166(00)00442-0

  日期：2000.11

  Penicillin acylase from Alcaligenes faecalis catalyzes the enantioselective acylation of amines with phenylacetamide in a kinetically controlled reaction in water at pH II. Addition of cosolvent to the reaction mixture significantly improved the enantioselectivity in most cases. Penicillin acylase from E. coli also catalyzed the phenylacetylation of amines, but an order of magnitude less efficiently than with the enzyme of A. faecalis. Amine resolution via kinetically controlled acylation competes effectively with hydrolysis of N-acylated compounds and constitutes a synthetically useful alternative to existing lipase-based methods. (C) 2000 Elsevier Science Ltd. All rights reserved.