11-HETE | 73151-66-3

• 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: 11-HETE
• 英文别名: 11-Hydroxyicosa-5,8,12,14-tetraenoic acid
• CAS: 73151-66-3
• 化学式: C₂₀H₃₂O₃
• 分子量: 320.472
• InChiKey: GCZRCCHPLVMMJE-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.2
• 重原子数：
  23
• 可旋转键数：
  14
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  57.5
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  11-HETE 、 三甲基硅烷化重氮甲烷 以 正己烷 为溶剂， 反应 0.17h， 生成 Methyl 11-hydroxyicosa-5,8,12,14-tetraenoate
  参考文献：
  名称：

  海藻Ulva的海洋藻类11-脂氧合酶的表征和固定化

  摘要：

  AbstractThe lipoxygenase (LOX) of the marine green alga Ulva fasciata was purified and immobilized in order to improve the stability and reusability. The algal LOX was partially purified by fractionation with 35–55% saturation of ammonium sulfate and MacroPrep high Q anion exchange chromatography. The LOX was purified ten times using linoleic acid (C18:2) or arachidonic acid (C20:4) as substrate, the Michaelis constant (Km) of LOX was 117.6, 31.3 μM, and maximum velocity (Vmax) was 12.8, 23.3 μmol hydroperoxy fatty acid/min‐mg protein, respectively. The algal LOX showed the highest activity towards C18:4 followed by C20:4, C18:2 and methyl ester of C18:4. LOX activity increased up to 10.5 times with increased concentration of Triton X‐100 in the extraction medium reaching an optimum at 0.05%. Calcium chloride, glutathione and phenylmethylsulphonyl fluoride were found effective protectants to LOX during purification. Hydroperoxyeicosatetraenoic acid (HpETE) formed from arachidonic acid catalyzed by this purified algal LOX was reduced and identified as 11‐hydroxy‐5,8,12,14‐eicosatetraenoic acid (11‐HETE) by NP‐HPLC and GC–MS. This algal 11‐LOX was immobilized in alginate beads. The stability was sevenfold greater than that of the unbound lipoxygenase at 4 °C in 0.05 M Tris–HCl buffer (pH 7.5). This is the first report on immobilization of a marine algal lipoxygenase with a view to its potential role in seafood flavor formation.

  DOI：

  10.1007/s11746-008-1262-6

文献信息

• A new antiangiogenic C24 oxylipin from the soft coral Sinularia numerosa
  作者：Takahiro Yamashita、Yoichi Nakao、Shigeki Matsunaga、Tsutomu Oikawa、Yukimitsu Imahara、Nobuhiro Fusetani

  DOI：10.1016/j.bmc.2008.10.083

  日期：2009.3

  A new oxylipin, 15-hydroxy-tetracosa-6,9,12,16,18-pentaenoic acid (15-HTPE; 1) was isolated as an inhibitor of tube-formation from the soft coral Sinularia numerosa. Its structure was elucidated by means of spectral analysis and chemical degradation. 15-HTPE inhibited tube formation of EA.hy926 cells at the concentration of 20–40 μM.

  从软珊瑚Sinularia numerosa中分离出了一种新的脂蛋白，15-羟基-四粘膜-6,9,12,16,18-戊烯酸（15-HTPE; 1）作为管形成的抑制剂。通过光谱分析和化学降解阐明了其结构。15-HTPE在20–40μM的浓度下可抑制EA.hy926细胞的管形成。
• Characterization and Immobilization of Marine Algal 11-Lipoxygenase from Ulva fasciata
  作者：Cheng Jung Tsai、Wu Feng Li、Bonnie Sun Pan

  DOI：10.1007/s11746-008-1262-6

  日期：2008.8

  AbstractThe lipoxygenase (LOX) of the marine green alga Ulva fasciata was purified and immobilized in order to improve the stability and reusability. The algal LOX was partially purified by fractionation with 35–55% saturation of ammonium sulfate and MacroPrep high Q anion exchange chromatography. The LOX was purified ten times using linoleic acid (C18:2) or arachidonic acid (C20:4) as substrate, the Michaelis constant (Km) of LOX was 117.6, 31.3 μM, and maximum velocity (Vmax) was 12.8, 23.3 μmol hydroperoxy fatty acid/min‐mg protein, respectively. The algal LOX showed the highest activity towards C18:4 followed by C20:4, C18:2 and methyl ester of C18:4. LOX activity increased up to 10.5 times with increased concentration of Triton X‐100 in the extraction medium reaching an optimum at 0.05%. Calcium chloride, glutathione and phenylmethylsulphonyl fluoride were found effective protectants to LOX during purification. Hydroperoxyeicosatetraenoic acid (HpETE) formed from arachidonic acid catalyzed by this purified algal LOX was reduced and identified as 11‐hydroxy‐5,8,12,14‐eicosatetraenoic acid (11‐HETE) by NP‐HPLC and GC–MS. This algal 11‐LOX was immobilized in alginate beads. The stability was sevenfold greater than that of the unbound lipoxygenase at 4 °C in 0.05 M Tris–HCl buffer (pH 7.5). This is the first report on immobilization of a marine algal lipoxygenase with a view to its potential role in seafood flavor formation.