| 1480426-86-5

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑烷类
• CAS: 1480426-86-5
• 化学式: C₁₆H₁₉NO₄
• 分子量: 290.323
• InChiKey: IPQNHSZWDFUYBH-UDCULWQZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.19
• 重原子数：
  21.0
• 可旋转键数：
  5.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  63.68
• 氢给体数：
  0.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  在 zinc(II) tetrahydroborate 、 双氧水 、 lithium hydroxide 作用下， 以 四氢呋喃 、 乙醚 、 水 为溶剂， 反应 2.75h， 生成 [2-²H]-(2R,3S)-2-methyl-3-hydroxypentanoic acid
  参考文献：
  名称：

  Coupled Methyl Group Epimerization and Reduction by Polyketide Synthase Ketoreductase Domains. Ketoreductase-Catalyzed Equilibrium Isotope Exchange

  摘要：

  Incubation of [2-H-2]-(2S,3R)-2-methyl-3-hydroxypentanoyl-SACP ([2-H-2]-1a) with the epimerizing ketoreductase domain EryKR1 in the presence of a catalytic amount NADP(+) (0.05 equiv) resulted in time- and cofactor-dependent washout of deuterium from la, as a result of equilibrium isotope exchange of transiently generated [2-H-2]-2-methyl-3-ketopentanoyl-ACP. Incubations of [2-H-2]-(2S,3S)-2-methyl-3-hydroxy-pentanoyl-SACP with RifKR7 and with NysKR1 also resulted in time-dependent loss of deuterium. By contrast, incubations of [2-H-2]-(2R,3S)-2-methyl-3-hydroxypentanoyl-SACP and [2-H-2]-(2R,3R)-2-methyl-3-hydroxypentanoyl-SACP with the non-epimerizing ketoreductase domains EryKR6 and TylKR1, respectively, did not result in any significant washout of deuterium. The isotope exchange assay directly establishes that specific polyketide synthase ketoreductase domains also have an intrinsic epimerase activity, thus enabling mechanistic analysis of a key determinant of polyketide stereocomplexity.

  DOI：

  10.1021/ja408944s
• 作为产物：
  描述：

  3-[2-2H2]-propionyl-(4S)-4-benzyl-1,3-oxazolidin-2-one 、 丙酰氯 在 lithium diisopropyl amide 作用下， 以 四氢呋喃 、 正庚烷 为溶剂， 反应 3.0h， 生成
  参考文献：
  名称：

  Coupled Methyl Group Epimerization and Reduction by Polyketide Synthase Ketoreductase Domains. Ketoreductase-Catalyzed Equilibrium Isotope Exchange

  摘要：

  Incubation of [2-H-2]-(2S,3R)-2-methyl-3-hydroxypentanoyl-SACP ([2-H-2]-1a) with the epimerizing ketoreductase domain EryKR1 in the presence of a catalytic amount NADP(+) (0.05 equiv) resulted in time- and cofactor-dependent washout of deuterium from la, as a result of equilibrium isotope exchange of transiently generated [2-H-2]-2-methyl-3-ketopentanoyl-ACP. Incubations of [2-H-2]-(2S,3S)-2-methyl-3-hydroxy-pentanoyl-SACP with RifKR7 and with NysKR1 also resulted in time-dependent loss of deuterium. By contrast, incubations of [2-H-2]-(2R,3S)-2-methyl-3-hydroxypentanoyl-SACP and [2-H-2]-(2R,3R)-2-methyl-3-hydroxypentanoyl-SACP with the non-epimerizing ketoreductase domains EryKR6 and TylKR1, respectively, did not result in any significant washout of deuterium. The isotope exchange assay directly establishes that specific polyketide synthase ketoreductase domains also have an intrinsic epimerase activity, thus enabling mechanistic analysis of a key determinant of polyketide stereocomplexity.

  DOI：

  10.1021/ja408944s