trans-3-hexylthio-2-propenoic acid | 120808-81-3

• 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: trans-3-hexylthio-2-propenoic acid
• 英文别名: (E)-4-thia-2-decenoic acid；(E)-3-hexylsulfanylprop-2-enoic acid
• CAS: 120808-81-3
• 化学式: C₉H₁₆O₂S
• 分子量: 188.291
• InChiKey: GJYQQZGYPSWXDL-SOFGYWHQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  12
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  62.6
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  1-己硫醇 在 sodium hydroxide 、 水 、 sodium ethanolate 作用下， 以 甲醇 为溶剂， 反应 17.02h， 生成 trans-3-hexylthio-2-propenoic acid
  参考文献：
  名称：

  Lipoxygenase-1 Inhibition with a Series of Half-Product Analogs

  摘要：

  A new series of sulfur-containing competitive inhibitors for lipoxygenase-1 from soybeans has been synthesized and characterized. The compounds resemble the omega-half of the product of catalysis, and can, therefore, be thought of as half-product analogs. A series of inhibitors differing in the length of the omega-terminal aliphatic substituent was assembled. Lipoxygenase-1 inhibition at pH 9 was greatest for (E)-4-thia-2-undecenal, the compound bearing the n-C7H15 substituent. Longer or shorter aliphatic substituents provided less effective inhibitors. This optimal fit of the inhibitory compounds reflecting the known substrate specificity of the enzyme along with the competitive inhibition kinetics displayed by these substances implicated an active site interaction. The relatively uncomplicated features of the compounds made it possible to explore synthetically for other aspects of the structure favorable for an inhibitory effect. Compounds containing functional groups other than the aldehyde at the 1-position were all less effective inhibitors. In addition to the optimal hydrophobic substituent, an electron-rich region in the molecule was also critical to the inhibitory effect. alpha,beta-Unsaturated aldehydes were about 10 times more effective inhibitors than the saturated analogs. The 4-thia substituent was not absolutely required for inhibition, but electron density at this position was important. gamma,delta-Unsaturation replaced the sulfur in this capacity with little effect on the inhibition constant. The electron-rich aldehydes showed no tendency to form hydrates in aqueous solution or Schiff base adducts with the enzyme. Physical evidence for a protein-ligand interaction was sought in a series of H-1 NMR spectroscopy experiments. There was clear evidence for a specific interaction between the compounds and the enzyme in these measurements. (C) 1996 Academic Press, Inc.

  DOI：

  10.1006/bioo.1996.0010

文献信息

• Volkova, K. A.; Levanova, E. P.; Voklov, A. N., Journal of Organic Chemistry USSR (English Translation), 1988, vol. 24, # 7, p. 1242 - 1245
  作者：Volkova, K. A.、Levanova, E. P.、Voklov, A. N.

  DOI：——

  日期：——
• VOLKOVA, K. A.;LEVANOVA, E. P.;VOLKOV, A. N., ZH. ORGAN. XIMII, 24,(1988) N 7, 1379-1382
  作者：VOLKOVA, K. A.、LEVANOVA, E. P.、VOLKOV, A. N.

  DOI：——

  日期：——
• US4877899A
  申请人：——

  公开号：US4877899A

  公开（公告）日：1989-10-31
• Lipoxygenase-1 Inhibition with a Series of Half-Product Analogs
  作者：Zhenyu Zhu、Max O. Funk, Jr.

  DOI：10.1006/bioo.1996.0010

  日期：1996.3

  A new series of sulfur-containing competitive inhibitors for lipoxygenase-1 from soybeans has been synthesized and characterized. The compounds resemble the omega-half of the product of catalysis, and can, therefore, be thought of as half-product analogs. A series of inhibitors differing in the length of the omega-terminal aliphatic substituent was assembled. Lipoxygenase-1 inhibition at pH 9 was greatest for (E)-4-thia-2-undecenal, the compound bearing the n-C7H15 substituent. Longer or shorter aliphatic substituents provided less effective inhibitors. This optimal fit of the inhibitory compounds reflecting the known substrate specificity of the enzyme along with the competitive inhibition kinetics displayed by these substances implicated an active site interaction. The relatively uncomplicated features of the compounds made it possible to explore synthetically for other aspects of the structure favorable for an inhibitory effect. Compounds containing functional groups other than the aldehyde at the 1-position were all less effective inhibitors. In addition to the optimal hydrophobic substituent, an electron-rich region in the molecule was also critical to the inhibitory effect. alpha,beta-Unsaturated aldehydes were about 10 times more effective inhibitors than the saturated analogs. The 4-thia substituent was not absolutely required for inhibition, but electron density at this position was important. gamma,delta-Unsaturation replaced the sulfur in this capacity with little effect on the inhibition constant. The electron-rich aldehydes showed no tendency to form hydrates in aqueous solution or Schiff base adducts with the enzyme. Physical evidence for a protein-ligand interaction was sought in a series of H-1 NMR spectroscopy experiments. There was clear evidence for a specific interaction between the compounds and the enzyme in these measurements. (C) 1996 Academic Press, Inc.