(Z)-4-十一烯酸乙酯 | 39944-81-5

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 中文名称: (Z)-4-十一烯酸乙酯
• 英文名称: ethyl (4Z)-undec-4-enoate
• 英文别名: Ethyl (4z)-undec-4-enoate；ethyl (Z)-undec-4-enoate
• CAS: 39944-81-5
• 化学式: C₁₃H₂₄O₂
• 分子量: 212.332
• InChiKey: GLERIGFUXHFPKP-KTKRTIGZSA-N

物化性质

• 沸点：
  256℃
• 密度：
  0.883
• 闪点：
  77℃

计算性质

• 辛醇/水分配系数(LogP)：
  4.4
• 重原子数：
  15
• 可旋转键数：
  10
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.77
• 拓扑面积：
  26.3
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  (Z)-4-十一烯酸乙酯 在 lithium aluminium tetrahydride 作用下， 以 乙醚 为溶剂， 以90%的产率得到(Z)-4-十一烯-1-醇
  参考文献：
  名称：

  Vig, O. P.; Sharma, M. L.; Taneja, K. C., Indian Journal of Chemistry - Section B Organic and Medicinal Chemistry, 1981, vol. 20, # 10, p. 863 - 865

  摘要：

  DOI：
• 作为产物：
  描述：

  (Z)-1-bromonon-2-ene 在 水 、 sodium chloride 作用下， 以 二甲基亚砜 、 苯 为溶剂， 反应 24.0h， 生成 (Z)-4-十一烯酸乙酯
  参考文献：
  名称：

  Vig, O. P.; Sharma, M. L.; Taneja, K. C., Indian Journal of Chemistry - Section B Organic and Medicinal Chemistry, 1981, vol. 20, # 10, p. 863 - 865

  摘要：

  DOI：

文献信息

• Fe-Catalyzed Synthesis of (13Z)-Eicos-13-en-10-one, the Main Sex Pheromone Component of Carposina niponensis
  作者：R. N. Shakhmaev、A. Sh. Sunagatullina、V. V. Zorin

  DOI：10.1007/s10600-017-1925-3

  日期：2017.1

  (13Z)-Eicos-13-en-10-one, the main sex pheromone component of Carposina niponensis, was synthesized stereoselectively via Fe-catalyzed cross-coupling of ethyl (4Z)-5-chloropent-4-enoate with hexylmagnesiumbromide to give ethyl (4Z)-undec-4-enoate and repeated Fe-catalyzed cross-coupling of its acid chloride with nonylmagnesiumbromide.

  (4Z)-5-氯戊-4-烯酸乙酯与溴化己基镁在铁催化下发生交叉偶联，得到(4Z)-十一-4-烯酸乙酯，然后其酰氯与溴化壬基镁在铁催化下重复发生交叉偶联，立体选择性地合成了(13Z)-二十烷-13-烯-10-酮（尼泊金鲫的主要性信息素成分）。
• Fe-catalyzed synthesis of (4Z)-alkenoates
  作者：R. N. Shakhmaev、A. Sh. Sunagatullina、V. V. Zorin

  DOI：10.1134/s1070363217030306

  日期：2017.3

  A new approach to stereoselective synthesis of (4Z)-alkenoates has been developed based on Fecatalyzed cross-coupling of ethyl (4Z)-5-chloropent-4-enoate with the Grignard reagents.
• Chemistry and Photochemistry Attending the Inactivation of Escherichia coli .beta.-Hydroxydecanoyl Thiol Ester Dehydrase by an Acetylenic Diazoketone
  作者：Barry S. Henderson、Barbara S. Larsen、John M. Schwab

  DOI：10.1021/ja00091a001

  日期：1994.6

  beta-Hydroxydecanoyl thiol ester dehydrase from Escherichia coli, an enzyme that catalyzes both dehydration and allylic rearrangement reactions, has been shown previously to undergo mechanism-based inactivation by the acetylenic substrate analog 1-diazo-4-undecyn-2-one (DUO). Details of the chemistry and photochemistry of DUO are now presented. Analysis of DUO-inactivated dehydrase by N-15 NMR spectroscopy indicates that DUO quantitatively alkylates histidine-70. Long-wavelength photoirradiation leads to spectrophotometrically observable changes in the DUO-dehydrase adduct. The structural changes were characterized by a combination of methods. Samples of protein that had been inactivated with [1-C-13]-, [(2)-C-13]-, and [3-C-13]DUO were analyzed by C-13 NMR spectroscopy, both prior and subsequent to photoirradiation. By comparisons of the chemical shifts of the enriched atoms of the inactivator moiety with those of model compounds, it was confirmed that the alpha-diazoketone moiety is retained in DUO-inactivated dehydrase and that photoirradiation leads to Wolff rearrangement of the alpha-diazoketone moiety followed by attack of a nucleophile on the resulting ketene. Proteolytic degradation of photoirradiated; DUO-inactivated dehydrase gave peptides that were analyzed by Edman sequencing and by mass spectrometry. The results are consistent with a single protein modification (at H70), and attack on the ketene by water, leading to a carboxylic acid. Samples of intact native, DUO-inactivated, and photoirradiated, DUO-inactivated dehydrase were analyzed by electrospray ionization mass spectrometry, the results of which clearly support the hypothesis that the ketene suffers attack by water. In light of recent results from X-ray crystallography, it is proposed that the water that attacks the ketene is one of two bound water molecules with specific roles in the binding and/or catalytic turnover of substrate. A Michael addition-elimination mechanism is presented to explain the unexpected hydrolytic lability of the DUO-dehydrase adduct.
• Vig, O. P.; Sharma, M. L.; Taneja, K. C., Indian Journal of Chemistry - Section B Organic and Medicinal Chemistry, 1981, vol. 20, # 10, p. 863 - 865
  作者：Vig, O. P.、Sharma, M. L.、Taneja, K. C.、Malik, Neera

  DOI：——

  日期：——