1-Stearoyl-2-docosahexaenoyl-sn-glycerol | 65886-80-8

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 甘油脂
• 英文名称: 1-Stearoyl-2-docosahexaenoyl-sn-glycerol
• 英文别名: [(2S)-1-hydroxy-3-octadecanoyloxypropan-2-yl] (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate
• CAS: 65886-80-8
• 化学式: C₄₃H₇₂O₅
• 分子量: 669.042
• InChiKey: LBDXVTOFXXDOGH-KXYFHQNYSA-N

物化性质

• 沸点：
  707.2±60.0 °C(Predicted)
• 密度：
  0.949±0.06 g/cm3(Predicted)
• 物理描述：
  Solid

计算性质

• 辛醇/水分配系数(LogP)：
  14.2
• 重原子数：
  48
• 可旋转键数：
  36
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  72.8
• 氢给体数：
  1
• 氢受体数：
  5

安全信息

• WGK Germany：
  3

反应信息

• 作为反应物：
  描述：

  2,3:4,5-di-O-cyclohexylidene-6-O-(p-methoxybenzyl)-D-myo-inositol 、 1-Stearoyl-2-docosahexaenoyl-sn-glycerol 在 吡啶 、 三乙胺 、 三氟乙酸 、 三氯氧磷 作用下， 生成 (4Z,7Z,10Z,13Z,16Z,19Z)-Docosa-4,7,10,13,16,19-hexaenoic acid (R)-2-[hydroxy-((1S,2R,3R,4S,5S,6R)-2,3,4,5,6-pentahydroxy-cyclohexyloxy)-phosphoryloxy]-1-octadecanoyloxymethyl-ethyl ester
  参考文献：
  名称：

  Enzymatic Synthesis of Phosphatidylinositol Bearing Polyunsaturated Acyl Group

  摘要：

  开发了一种合成具有多不饱和脂肪酰基的磷脂酰肌醇（PI）的新路线，采用脂肪酶和磷脂酶C作为生物催化剂，以补充正常的化学反应。

  DOI：

  10.1271/bbb.60.1916
• 作为产物：
  描述：

  1-stearoyl-2-benzylglycerophosphocholine 在 4-二甲氨基吡啶 、 Tris-HCl buffer 、 sodium salt of choleic acid 、 phosphalipase C 、 N,N'-二环己基碳二亚胺 、 calcium chloride 作用下， 以 氯仿 为溶剂， 生成 1-Stearoyl-2-docosahexaenoyl-sn-glycerol
  参考文献：
  名称：

  Enzymatic Synthesis of Phosphatidylinositol Bearing Polyunsaturated Acyl Group

  摘要：

  开发了一种合成具有多不饱和脂肪酰基的磷脂酰肌醇（PI）的新路线，采用脂肪酶和磷脂酶C作为生物催化剂，以补充正常的化学反应。

  DOI：

  10.1271/bbb.60.1916

文献信息

• Substrate specificity of diacylglycerol kinase-epsilon and the phosphatidylinositol cycle
  作者：Yulia V. Shulga、Matthew K. Topham、Richard M. Epand

  DOI：10.1016/j.febslet.2011.11.016

  日期：2011.12.15

  We show that diacylglycerol kinase-epsilon (DGK epsilon) has less preference for the acyl chain at the sn-1 position of diacylglycerol (DAG) than the one at the sn-2 position. Although DGK epsilon discriminates between 1-stearoyl-2-arachidonoyl-DAG and 1-palmitoyl-2-arachidonoyl-DAG, it has similar substrate preference for 1-stearoyl-2-arachidonoyl-DAG and 1,2-diarachidonoyl-DAG. We suggest that in addition to binding to the enzyme, the acyl chain at the sn-1 position may contribute to the depth of insertion of the DAG into the membrane. Thus, the DAG intermediate of the PI-cycle, 1-stearoyl-2-arachidonoyl-DAG, is not the only DAG that is a good substrate for DGKe, the DGK isoform involved in PI-cycling. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
• Characterization of the Human LPIN1-encoded Phosphatidate Phosphatase Isoforms
  作者：Gil-Soo Han、George M. Carman

  DOI：10.1074/jbc.m110.117747

  日期：2010.5

  The human LPIN1 gene encodes the protein lipin 1, which possesses phosphatidate (PA) phosphatase (3-sn-phosphatidate phosphohydrolase; EC 3.1.3.4) activity (Han, G.-S., Wu, W.-I., and Carman, G. M. (2006) J. Biol. Chem. 281, 9210-9218). In this work, we characterized human lipin 1 alpha, beta, and gamma isoforms that were expressed in Escherichia coli and purified to near homogeneity. PA phosphatase activities of the alpha, beta, and gamma isoforms were dependent on Mg2+ or Mn2+ ions at pH 7.5 at 37 degrees C. The activities were inhibited by concentrations of Mg2+ and Mn2+ above their optimums and by Ca2+, Zn2+, N-ethylmaleimide, propranolol, and the sphingoid bases sphingosine and sphinganine. The activities were thermally labile at temperatures above 40 degrees C. The alpha, beta, and gamma activities followed saturation kinetics with respect to the molar concentration of PA (K-m values of 0.35, 0.24, and 0.11 mM, respectively) but followed positive cooperative (Hill number similar to 2) kinetics with respect to the surface concentration of PA (K-m values of 4.2, 4.5, and 4.3 mol %, respectively) in Triton X-100/PA-mixed micelles. The turnover numbers (k(cat)) for the alpha, beta, and gamma isoforms were 68.8 +/- 3.5, 42.8 +/- 2.5, and 5.7 +/- 0.2 s(-1), respectively, whereas their energy of activation values were 14.2, 15.5, and 18.5 kcal/mol, respectively. The isoform activities were dependent on PA as a substrate and required at least one unsaturated fatty acyl moiety for maximum activity.