methyl pentadecanoate-2,2-d2 | 169449-81-4

• 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: methyl pentadecanoate-2,2-d2
• CAS: 169449-81-4
• 化学式: C₁₆H₃₂O₂
• 分子量: 258.413
• InChiKey: XIUXKAZJZFLLDQ-DOBBINOXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.25
• 重原子数：
  18.0
• 可旋转键数：
  13.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.94
• 拓扑面积：
  26.3
• 氢给体数：
  0.0
• 氢受体数：
  2.0

反应信息

• 作为反应物：
  描述：

  methyl pentadecanoate-2,2-d2 在 lithium aluminium tetrahydride 、 Amberlyst 15 、 硫酸 、 氢溴酸 、 magnesium 作用下， 以 四氢呋喃 为溶剂， 生成
  参考文献：
  名称：

  Dihydroceramide Δ⁴ Desaturase Initiates Substrate Oxidation at C-4

  摘要：

  The intermolecular primary deuterium isotope effects on the individual C-H bond cleavage steps involved in dihydroceramide Delta (4) desaturation have been determined for the first time by incubating rat liver microsomes with 1:1 mixtures of nonlabeled substrate and the appropriate regiospecifically dideutelatred analogue. Analysis of the enzymatic products via gas chromatography coupled to mass spectrometry showed that the introduction of the (E) double bond between C-4 and C-5 occurs in two discrete steps: cleavage of the C-4-H bond was found to be very sensitive to isotopic substitution (k(H)/k(D) = 8.0 +/- 0 8). while a negligible isotope effect (k(H)/k(D) = 1.02 +/- 0.07) was observed for the C-5-H bond-breaking step. According to a mechanistic model that we have previously proposed, these results suggest that initial oxidation for this desaturation reaction occurs at C-4. This finding correlates nicely with the observation that 4-hydroxylated products are produced from a similar substrate by a closely related oxidative enzyme in yeast.

  DOI：

  10.1021/ja010088w
• 作为产物：
  描述：

  十五烷酸甲酯 在 氘代甲醇-d 、 sodium 作用下， 生成 methyl pentadecanoate-2,2-d2
  参考文献：
  名称：

  Dihydroceramide Δ⁴ Desaturase Initiates Substrate Oxidation at C-4

  摘要：

  The intermolecular primary deuterium isotope effects on the individual C-H bond cleavage steps involved in dihydroceramide Delta (4) desaturation have been determined for the first time by incubating rat liver microsomes with 1:1 mixtures of nonlabeled substrate and the appropriate regiospecifically dideutelatred analogue. Analysis of the enzymatic products via gas chromatography coupled to mass spectrometry showed that the introduction of the (E) double bond between C-4 and C-5 occurs in two discrete steps: cleavage of the C-4-H bond was found to be very sensitive to isotopic substitution (k(H)/k(D) = 8.0 +/- 0 8). while a negligible isotope effect (k(H)/k(D) = 1.02 +/- 0.07) was observed for the C-5-H bond-breaking step. According to a mechanistic model that we have previously proposed, these results suggest that initial oxidation for this desaturation reaction occurs at C-4. This finding correlates nicely with the observation that 4-hydroxylated products are produced from a similar substrate by a closely related oxidative enzyme in yeast.

  DOI：

  10.1021/ja010088w