1,2-Dioleoyl-3-linoleoyl-sn-glycerol | 72120-34-4

• 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: 1,2-Dioleoyl-3-linoleoyl-sn-glycerol
• 英文别名: [(2R)-3-[(9Z,12Z)-octadeca-9,12-dienoyl]oxy-2-[(Z)-octadec-9-enoyl]oxypropyl] (Z)-octadec-9-enoate
• CAS: 72120-34-4
• 化学式: C₅₇H₁₀₂O₆
• 分子量: 883.4
• InChiKey: JTMWOTXEVWLTTO-YKZMILTLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  21.7
• 重原子数：
  63
• 可旋转键数：
  52
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.81
• 拓扑面积：
  78.9
• 氢给体数：
  0
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  1,2-二油酰基-sn-甘油 、 L-(+)-2-Linoleoyl-3-oleoyl-glycerin-1-phosphorsaeure-(2-amino-aethylester) 生成 1,2-Dioleoyl-3-linoleoyl-sn-glycerol 、 1-油酰基-2-羟基-sn-甘油-3-磷酸乙醇胺
  参考文献：
  名称：

  Saccharomyces cerevisiae phospholipid:diacylglycerol acyl transferase (PDAT) devoid of its membrane anchor region is a soluble and active enzyme retaining its substrate specificities

  摘要：

  A N-terminal deleted version of the Saccharomyces cerevisiae phospholipid:diacylglycerol acyltransferase (ScPDAT), lacking the predicted membrane-spanning region, was fused in frame with alpha-factor secretion signal and expressed in Pichia pastoris under the control of the methanol inducible alcohol oxidase promoter. This resulted in a truncated, soluble and highly active PDAT protein secreted into the culture medium of the recombinant cells. The soluble as well as native membrane bound enzymes was shown to be glycosylated and extensive deglycosylation severely lowered the activity. The production of a soluble and extracellular PDAT allowed us to investigate substrate preferences of the enzyme without interference of endogenous lipids and enzymes. Similar to the membrane bound counterpart, the highest activity was achieved with acyl groups at sn-2 position of phosphatidylethanolamine as acyl donor and 1,2-diacylglycerols as acyl acceptor. The soluble enzyme was also able to catalyze, at a low rate, a number of transacylation reactions between various neutral lipids and between polar lipids and neutral lipids others than diacylglycerols, including acylation of long chain alcohols. (c) 2007 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.bbalip.2007.10.007

文献信息

• Kawasaki T.; Snyder F., J Biol Chem, 1988, 0021-9258, 2593-6
  作者：Kawasaki T.、Snyder F.

  DOI：——

  日期：——
• Saccharomyces cerevisiae phospholipid:diacylglycerol acyl transferase (PDAT) devoid of its membrane anchor region is a soluble and active enzyme retaining its substrate specificities
  作者：Alokesh Ghosal、Antoni Banas、Ulf Ståhl、Anders Dahlqvist、Ylva Lindqvist、Sten Stymne

  DOI：10.1016/j.bbalip.2007.10.007

  日期：2007.12

  A N-terminal deleted version of the Saccharomyces cerevisiae phospholipid:diacylglycerol acyltransferase (ScPDAT), lacking the predicted membrane-spanning region, was fused in frame with alpha-factor secretion signal and expressed in Pichia pastoris under the control of the methanol inducible alcohol oxidase promoter. This resulted in a truncated, soluble and highly active PDAT protein secreted into the culture medium of the recombinant cells. The soluble as well as native membrane bound enzymes was shown to be glycosylated and extensive deglycosylation severely lowered the activity. The production of a soluble and extracellular PDAT allowed us to investigate substrate preferences of the enzyme without interference of endogenous lipids and enzymes. Similar to the membrane bound counterpart, the highest activity was achieved with acyl groups at sn-2 position of phosphatidylethanolamine as acyl donor and 1,2-diacylglycerols as acyl acceptor. The soluble enzyme was also able to catalyze, at a low rate, a number of transacylation reactions between various neutral lipids and between polar lipids and neutral lipids others than diacylglycerols, including acylation of long chain alcohols. (c) 2007 Elsevier B.V. All rights reserved.