(9Z)-12-hydroxy-9-dodecenoic acid ethyl ester | 79894-08-9

• 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: (9Z)-12-hydroxy-9-dodecenoic acid ethyl ester
• 英文别名: ethyl (9Z)-12-hydroxy-9-dodecenate；ethyl (Z)-12-hydroxydodec-9-enoate
• CAS: 79894-08-9
• 化学式: C₁₄H₂₆O₃
• 分子量: 242.359
• InChiKey: PFGWTCJGGAZASY-CLFYSBASSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.5
• 重原子数：
  17
• 可旋转键数：
  12
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  46.5
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (9Z)-12-hydroxy-9-dodecenoic acid ethyl ester 在 VinP₄ polyketide synthase thioesterase domain 作用下， 以 二甲基亚砜 为溶剂， 反应 24.0h， 以51%的产率得到(10Z,23Z)-1,14-dioxacyclohexacosa-10,23-diene-2,15-dione
  参考文献：
  名称：

  Potent Oligomerization and Macrocyclization Activity of the Thioesterase Domain of Vicenistatin Polyketide Synthase

  摘要：

  The thioesterase domain of the polyketide synthase involved in the biosynthesis of the 20-membered macrolactam antibiotic vicenistatin (VinTE) was found to catalyze oligomerization and macrocyclization of omega-hydroxy fatty acid ethyl esters to afford 17-28-membered macrocyclic lactones. The ring sizes of the macrocycles appear to be limited to the more moderate sizes because of the space limitation of the active site of VinTE. It was also verified that the initially formed linear dimer is first released from the active site of VinTE and then is recognized again by VinTE prior to its transformation to the cyclic dimer.

  DOI：

  10.1055/s-0031-1290385
• 作为产物：
  描述：

  油酸乙酯 在 双(三甲基硅烷基)氨基钾 、 对甲苯磺酸 、 臭氧 作用下， 以 乙醇 、 二氯甲烷 、 甲苯 为溶剂， 反应 28.0h， 生成 (9Z)-12-hydroxy-9-dodecenoic acid ethyl ester
  参考文献：
  名称：

  Potent Oligomerization and Macrocyclization Activity of the Thioesterase Domain of Vicenistatin Polyketide Synthase

  摘要：

  The thioesterase domain of the polyketide synthase involved in the biosynthesis of the 20-membered macrolactam antibiotic vicenistatin (VinTE) was found to catalyze oligomerization and macrocyclization of omega-hydroxy fatty acid ethyl esters to afford 17-28-membered macrocyclic lactones. The ring sizes of the macrocycles appear to be limited to the more moderate sizes because of the space limitation of the active site of VinTE. It was also verified that the initially formed linear dimer is first released from the active site of VinTE and then is recognized again by VinTE prior to its transformation to the cyclic dimer.

  DOI：

  10.1055/s-0031-1290385

文献信息

• US4350703A
  申请人：——

  公开号：US4350703A

  公开（公告）日：1982-09-21
• Potent Oligomerization and Macrocyclization Activity of the Thioesterase Domain of Vicenistatin Polyketide Synthase
  作者：Tadashi Eguchi、Fumitaka Kudo、Yusaku Asou、Moe Watanabe、Takashi Kitayama

  DOI：10.1055/s-0031-1290385

  日期：2012.7

  The thioesterase domain of the polyketide synthase involved in the biosynthesis of the 20-membered macrolactam antibiotic vicenistatin (VinTE) was found to catalyze oligomerization and macrocyclization of omega-hydroxy fatty acid ethyl esters to afford 17-28-membered macrocyclic lactones. The ring sizes of the macrocycles appear to be limited to the more moderate sizes because of the space limitation of the active site of VinTE. It was also verified that the initially formed linear dimer is first released from the active site of VinTE and then is recognized again by VinTE prior to its transformation to the cyclic dimer.