DG(20:0/20:4(5Z,8Z,11Z,14Z)/0:0)

• 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: DG(20:0/20:4(5Z,8Z,11Z,14Z)/0:0)
• 英文别名: [(2S)-3-hydroxy-2-[(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoyl]oxypropyl] icosanoate
• 化学式: C₄₃H₇₆O₅
• 分子量: 673.1
• InChiKey: OUGXERRDRINUQU-AICYSBPGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  15.4
• 重原子数：
  48
• 可旋转键数：
  38
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.77
• 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：

  DG(20:0/20:4(5Z,8Z,11Z,14Z)/0:0) 、 adenosine 5'-triphosphate 生成 1-Arachidoyl-2-arachidonoyl-sn-glycero-3-phosphate(2-) 、 adenosine 5'-diphosphate 、 氢(+1)阳离子
  参考文献：
  名称：

  Diacylglycerol Kinase ϵ Is Selective for Both Acyl Chains of Phosphatidic Acid or Diacylglycerol

  摘要：

  The phosphatidylinositol ( PI) cycle mediates many cellular events by controlling the metabolism of many lipid second messengers. Diacylglycerol kinase epsilon (DGK epsilon) has an important role in this cycle. DGK epsilon is the only DGK isoform to show inhibition by its product phosphatidic acid (PA) as well as substrate specificity for sn-2 arachidonoyl-diacylglycerol (DAG). Here, we show that this inhibition and substrate specificity are both determined by selectivity for a combination of the sn-1 and sn-2 acyl chains of PA or DAG, respectively, preferring the most prevalent acyl chain composition of lipids involved specifically in the PI cycle, 1-stearoyl-2-arachidonoyl. Although the difference in rate for closely related lipid species is small, there is a significant enrichment of 1-stearoyl-2-arachidonoyl PI because of the cyclical nature of PI turnover. Wealso show that the inhibition of DGK epsilon by PA is competitive and that the deletion of the hydrophobic segment and cationic cluster of DGK epsilon does not affect its selectivity for the acyl chains of PA or DAG. Thus, this active site not only recognizes the lipid headgroup but also a combination of the two acyl chains in PA or DAG. We propose a mechanism of DGK epsilon regulation where its dual acyl chain selectivity is used to negatively regulate its enzymatic activity in a manner that ensures DGK epsilon remains committed to the PI turnover cycle. This novel mechanism of enzyme regulation within a signaling pathway could serve as a template for the regulation of enzymes in other pathways in the cell.

  DOI：

  10.1074/jbc.m109.050617