1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycerol

• 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-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycerol
• 英文别名: [(2S)-1-hexadecanoyloxy-3-hydroxypropan-2-yl] (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate
• 化学式: C₄₁H₆₈O₅
• 分子量: 641.0
• InChiKey: BXVYQJJBMVVALQ-VVSMSMGFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  13.1
• 重原子数：
  46
• 可旋转键数：
  34
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.66
• 拓扑面积：
  72.8
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycerol 、 Cytidindiphosphatcholin 生成 1-棕榈酰-2-二十二碳六烯酰-Sn-甘油-3-磷酰胆碱 、 cytidine 5'-monophosphate 、 氢(+1)阳离子
  参考文献：
  名称：

  Henneberry A.L.; McMaster C.R., Biochem J, 1999, 0264-6021, 291-8

  摘要：

  DOI：
• 作为产物：
  描述：

  1-palmitoyl-2-[(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl]-sn-glycero-3-phosphate(2-) 、 水 生成 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycerol 、 H3PO4
  参考文献：
  名称：

  Characterization of the Human LPIN1-encoded Phosphatidate Phosphatase Isoforms

  摘要：

  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.

  DOI：

  10.1074/jbc.m110.117747

文献信息

• Cloning, Genomic Organization, and Characterization of a Human Cholinephosphotransferase
  作者：Annette L. Henneberry、Graeme Wistow、Christopher R. McMaster

  DOI：10.1074/jbc.m005786200

  日期：2000.9

  A cholinephosphotransferase activity catalyzes the final step in the de novo synthesis of phosphatidylcholine Dia the transfer of a phosphocholine moiety from CDP choline to diacylglycerol. Ethanolaminephosphotransferase activity catalyzes a similar reaction substituting CDP ethanolamine as the phosphobase donor. We report the identification and cloning of a human cDNA (human cholinephosphotransferase (hCPT1)) that codes for a cholinephosphotransferase-specific enzyme. This was demonstrated using in vitro enzyme assays and in vivo measurement of the reconstitution of the phosphatidylcholine and phosphatidylethanolamine biosynthetic pathways in yeast cells devoid of their own endogenous cholinephosphotransferase and ethanolaminephosphotransferase activities. This contrasted with our previously cloned human choline/ethanolaminephosphotransferase cDNA that was demonstrated to code for a dual specificity choline/ethanolaminephosphotransferase. The hCPT1 and human choline/ethanolaminephosphotransferase (hCEPT1) predicted amino acid sequences possessed 60% overall identity and had only one variation in the amino acid residues within the CDP-alcohol phosphotransferase catalytic motif, In vitro assessment of hCPT1 and hCEPT1 derived cholinephosphotransferase activities also revealed differences in diradylglycerol specificities including their capacity to synthesize platelet-activating factor and platelet-activating factor precursor. Expression of the hCPT1 mRNA varied greater than 100-fold between tissues and was most abundant in testis followed by colon, small intestine, heart, prostate, and spleen. This was in marked contrast to the hCEPT1 mRNA, which has been found in similar abundance in all tissues tested to date. Both the hCPT1 and hCEPT1 enzymes were able to reconstitute the synthesis of PC in yeast to levels provided by the endogenous yeast cholinephosphotransferase; however, only hCEPT1-derived activity was able to complement the yeast CPT1 gene in its interaction with SEC14 and affect cell growth.