S-(2-methyl-3-oxo-5,5,5-trifluoropentanoyl)-N-acetylcysteamine | 1402719-01-0

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: S-(2-methyl-3-oxo-5,5,5-trifluoropentanoyl)-N-acetylcysteamine
• CAS: 1402719-01-0
• 化学式: C₁₀H₁₄F₃NO₃S
• 分子量: 285.287
• InChiKey: SZZQMNJGSYCWCW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.54
• 重原子数：
  18.0
• 可旋转键数：
  6.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.7
• 拓扑面积：
  63.24
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  S-(2-methyl-3-oxo-5,5,5-trifluoropentanoyl)-N-acetylcysteamine 在 RifKR₇ 、 甘油 、 还原型辅酶II(NADPH)四钠盐 、 sodium chloride 作用下， 以 氘代二甲亚砜 为溶剂， 生成
  参考文献：
  名称：

  Monitoring Biocatalytic Transformations Mediated by Polyketide Synthase Enzymes in Cell Lysate via Fluorine NMR

  摘要：

  The biocatalytic employment of modular polyketide synthase enzymes in cell lysate has become a viable route to preparative quantities of synthetically valuable polyketide fragments. We report the quantitative, uninvasive, and continuous monitoring of such biocatalytic reactions by observing trifluoromethyl-bearing substrates via F-19 NMR spectroscopic analysis. To demonstrate the utility of this technique, we followed reactions catalyzed by a thioesterase and several ketoreductases.

  DOI：

  10.1055/s-0032-1316554
• 作为产物：
  描述：

  S-(3-oxo-5,5,5-trifluoropentanoyl)-N-acetylcysteamine 、 碘甲烷 在 potassium tert-butylate 作用下， 以 四氢呋喃 为溶剂， 以64%的产率得到S-(2-methyl-3-oxo-5,5,5-trifluoropentanoyl)-N-acetylcysteamine
  参考文献：
  名称：

  Monitoring Biocatalytic Transformations Mediated by Polyketide Synthase Enzymes in Cell Lysate via Fluorine NMR

  摘要：

  The biocatalytic employment of modular polyketide synthase enzymes in cell lysate has become a viable route to preparative quantities of synthetically valuable polyketide fragments. We report the quantitative, uninvasive, and continuous monitoring of such biocatalytic reactions by observing trifluoromethyl-bearing substrates via F-19 NMR spectroscopic analysis. To demonstrate the utility of this technique, we followed reactions catalyzed by a thioesterase and several ketoreductases.

  DOI：

  10.1055/s-0032-1316554