2-乙基-5-硝基-2,3-二氢(2-1b)咪唑并-噁唑 | 74581-83-2

• 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: 2-乙基-5-硝基-2,3-二氢(2-1b)咪唑并-噁唑
• 英文名称: 5-hydroperoxyeicosatetraenoic acid
• 英文别名: 5-Hydroperoxyicosa-6,8,11,14-tetraenoic acid
• CAS: 74581-83-2
• 化学式: C₂₀H₃₂O₄
• 分子量: 336.472
• InChiKey: JNUUNUQHXIOFDA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.3
• 重原子数：
  24
• 可旋转键数：
  15
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  66.8
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-乙基-5-硝基-2,3-二氢(2-1b)咪唑并-噁唑 在 吡啶 、 乙酸酐 作用下， 生成 (6E,8Z,11Z,14Z)-5-氧代-6,8,11,14-二十碳四烯酸
  参考文献：
  名称：

  Inhibitory and mechanistic investigations of oxo-lipids with human lipoxygenase isozymes

  摘要：

  Oxo-lipids, a large family of oxidized human lipoxygenase (hLOX) products, are of increasing interest to researchers due to their involvement in different inflammatory responses in the cell. Oxo-lipids are unique because they contain electrophilic sites that can potentially form covalent bonds through a Michael addition mechanism with nucleophilic residues in protein active sites and thus increase inhibitor potency. Due to the resemblance of oxo-lipids to LOX substrates, the inhibitor potency of 4 different oxo-lipids; 5-oxo-6,8,11,14-(E,Z,Z,Z)-eicosatetraenoic acid (5-oxo-ETE), 15-oxo-5,8,11,13-(Z,Z,Z,E)-eicosatetraenoic acid (15-oxo-ETE), 12-oxo-5,8,10,14-(Z,Z,E,Z)-eicosatetraenoic acid (12-oxo-ETE), and 13-oxo-9,11-(Z,E)-octadecadienoic acid (13-oxo-ODE) were determined against a library of LOX isozymes; leukocyte 5-lipoxygenase (h5-LOX), human reticulocyte 15-lipoxygenase-1 (h15-LOX-1), human platelet 12-lipoxygenase (h12-LOX), human epithelial 15-lipoxygenase-2 (h15-LOX-2), soybean 15-lipoxygenase-1 (s15-LOX-1), and rabbit reticulocyte 15-LOX (r15-LOX). 15-Oxo-ETE exhibited the highest potency against h12-LOX, with an IC50 = 1 +/- 0.1 mu M and was highly selective. Steady state inhibition kinetic experiments determined 15-oxo-ETE to be a mixed inhibitor against h12-LOX, with a K-ic value of 0.087 +/- 0.008 mu M and a K-iu value of 2.10 +/- 0.8 mu M. Time-dependent studies demonstrated irreversible inhibition with 12-oxo-ETE and h15-LOX-1, however, the concentration of 12-oxo-ETE required (K-i = 36.8 +/- 13.2 mu M) and the time frame (k(2) = 0.0019 +/- 0.00032 s(-1)) were not biologically relevant. These data are the first observations that oxo-lipids can inhibit LOX isozymes and may be another mechanism in which LOX products regulate LOX activity. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2014.05.025
• 作为产物：
  描述：

  花生四烯酸 在 脂肪氧化酶 、 磷酸肌酸 、 5’-三磷酸腺苷 、 calcium chloride 作用下， 反应 0.07h， 生成 2-乙基-5-硝基-2,3-二氢(2-1b)咪唑并-噁唑
  参考文献：
  名称：

  Detection of 5-Lipoxygenase Activity in the LiverwortMarchantia polymorphaL.

  摘要：

  我们通过光谱法和质谱法在多形小苔藓的均匀液中检测到了5-LOX（花生四烯酸5-脂氧化酶）。LC/MS/MS分析表明，苔藓植物的5-LOX以花生四烯酸为底物生成5-过氧基-6,8,11,14-二十碳四烯酸（5-HPETE）。5-LOX活性表现出对Ca2+的响应，这与人类5-LOX的结果一致。这些发现表明苔藓植物在防御信号反应中利用了花生四烯酸级联反应。

  DOI：

  10.1271/bbb.90479

文献信息

• Detection of 5-Lipoxygenase Activity in the Liverwort<i>Marchantia polymorpha</i>L.
  作者：Hirosuke KANAMOTO、Miho TAKEMURA、Kanji OHYAMA

  DOI：10.1271/bbb.90479

  日期：2009.11.23

  We detected 5-LOX (arachidonate 5-lipoxygenase) in the homogenate of Marchantia polymorpha by spectrophotometry and mass spectrometry. LC/MS/MS analysis indicated that the liverwort 5-LOX produced 5-hydroperoxy-6,8,11,14-eicosatetraenoic acid (5-HPETE) with arachidonic acid as a substrate. The 5-LOX activity showed a Ca2+ response, as demonstrated for human 5-LOX. These findings suggest that the liverwort utilizes an arachidonate cascade in a defense signal response.

  我们通过光谱法和质谱法在多形小苔藓的均匀液中检测到了5-LOX（花生四烯酸5-脂氧化酶）。LC/MS/MS分析表明，苔藓植物的5-LOX以花生四烯酸为底物生成5-过氧基-6,8,11,14-二十碳四烯酸（5-HPETE）。5-LOX活性表现出对Ca2+的响应，这与人类5-LOX的结果一致。这些发现表明苔藓植物在防御信号反应中利用了花生四烯酸级联反应。
• Inhibitory and mechanistic investigations of oxo-lipids with human lipoxygenase isozymes
  作者：Michelle M. Armstrong、Giovanni Diaz、Victor Kenyon、Theodore R. Holman

  DOI：10.1016/j.bmc.2014.05.025

  日期：2014.8

  Oxo-lipids, a large family of oxidized human lipoxygenase (hLOX) products, are of increasing interest to researchers due to their involvement in different inflammatory responses in the cell. Oxo-lipids are unique because they contain electrophilic sites that can potentially form covalent bonds through a Michael addition mechanism with nucleophilic residues in protein active sites and thus increase inhibitor potency. Due to the resemblance of oxo-lipids to LOX substrates, the inhibitor potency of 4 different oxo-lipids; 5-oxo-6,8,11,14-(E,Z,Z,Z)-eicosatetraenoic acid (5-oxo-ETE), 15-oxo-5,8,11,13-(Z,Z,Z,E)-eicosatetraenoic acid (15-oxo-ETE), 12-oxo-5,8,10,14-(Z,Z,E,Z)-eicosatetraenoic acid (12-oxo-ETE), and 13-oxo-9,11-(Z,E)-octadecadienoic acid (13-oxo-ODE) were determined against a library of LOX isozymes; leukocyte 5-lipoxygenase (h5-LOX), human reticulocyte 15-lipoxygenase-1 (h15-LOX-1), human platelet 12-lipoxygenase (h12-LOX), human epithelial 15-lipoxygenase-2 (h15-LOX-2), soybean 15-lipoxygenase-1 (s15-LOX-1), and rabbit reticulocyte 15-LOX (r15-LOX). 15-Oxo-ETE exhibited the highest potency against h12-LOX, with an IC50 = 1 +/- 0.1 mu M and was highly selective. Steady state inhibition kinetic experiments determined 15-oxo-ETE to be a mixed inhibitor against h12-LOX, with a K-ic value of 0.087 +/- 0.008 mu M and a K-iu value of 2.10 +/- 0.8 mu M. Time-dependent studies demonstrated irreversible inhibition with 12-oxo-ETE and h15-LOX-1, however, the concentration of 12-oxo-ETE required (K-i = 36.8 +/- 13.2 mu M) and the time frame (k(2) = 0.0019 +/- 0.00032 s(-1)) were not biologically relevant. These data are the first observations that oxo-lipids can inhibit LOX isozymes and may be another mechanism in which LOX products regulate LOX activity. (C) 2014 Elsevier Ltd. All rights reserved.