1-辛酰基-2-羟基-sn-甘油-3-磷酸胆碱 | 45287-18-1

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 甘油磷脂
• 中文名称: 1-辛酰基-2-羟基-sn-甘油-3-磷酸胆碱
• 英文名称: 1-octanoyl-sn-glycero-3-phosphocholine
• 英文别名: 1-Octanoyl-sn-glycero-3-phosphorylcholin；LPC (8:0)；[(2R)-2-hydroxy-3-octanoyloxypropyl] 2-(trimethylazaniumyl)ethyl phosphate
• CAS: 45287-18-1
• 化学式: C₁₆H₃₄NO₇P
• 分子量: 383.422
• InChiKey: ZVPMBHRQDPDKEF-OAHLLOKOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.2
• 重原子数：
  25
• 可旋转键数：
  16
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.94
• 拓扑面积：
  105
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  1-辛酰基-2-羟基-sn-甘油-3-磷酸胆碱 生成 1-Octanoyl-sn-glycero-2,3-cyclic phosphate 、 胆碱
  参考文献：
  名称：

  Phospholipase D Toxins of Brown Spider Venom Convert Lysophosphatidylcholine and Sphingomyelin to Cyclic Phosphates

  摘要：

  Loxosceles属棕蜘蛛的毒液中含有磷脂酶D酶毒素，可导致严重皮肤坏死，甚至导致人类死亡。这些毒素会分解哺乳动物组织中的鞘氨醇和溶血磷脂酰胆碱，释放胆碱头基。此前有报道称，分解底物的其他产物是单酯磷脂，这是底物水解的结果。我们使用31P NMR和质谱技术证明，重组毒素以及来自不同Loxosceles物种的完整毒液仅催化转磷酸化，而不是水解，从两种主要底物形成环状磷酸盐产物。环状磷酸盐与单酯磷酸盐具有截然不同的生物特性，可能与棕蜘蛛毒液致病有关。

  DOI：

  10.1371/journal.pone.0072372
• 作为产物：
  描述：

  (2R)-2,3-二(辛酰氧基)丙基2-(三甲基铵基)乙基磷酸酯 在 水 作用下， 以 various solvent(s) 为溶剂， 生成 1-辛酰基-2-羟基-sn-甘油-3-磷酸胆碱
  参考文献：
  名称：

  Secretory phospholipase A2-α from Arabidopsis thaliana: functional parameters and substrate preference

  摘要：

  The secretory phospholipase A(2)-alpha from Arabidopsis thaliana (AtsPLA(2)-alpha), being one of the first plant sPLA(2)s obtained in purified state, has been characterised with respect to substrate preference and optimum conditions of catalysis. The optima of pH, temperature, and calcium concentration were similar to the parameters of secretory PLA(2)s from animals. However, substrate preferences markedly differed. In contrast to pancreatic PLA(2)s, AtsPLA(2)-alpha preferred zwitterionic phospholipids, and showed lower activity toward anionic phospholipids. In substrates with two identical fatty acid chains, AtsPLA(2)-alpha showed optimum activity toward phospholipids with decanoyl groups. In substrates with palmitoyl groups in sn-1 position, acyl chains with higher degree of unsaturation in sn-2 position were preferred, excluding arachidonic acid, showing the evolutionary adaptation of the enzyme to substrate composition in plants. Km values for short chain phospholipids were comparable to sPLA(2)s from animals, whereas k(cat) values were much smaller and interfacial activation was less important. (C) 2007 Elsevier Ireland Ltd. All rights reserved.

  DOI：

  10.1016/j.chemphyslip.2007.07.001

文献信息

• Phospholipase D Toxins of Brown Spider Venom Convert Lysophosphatidylcholine and Sphingomyelin to Cyclic Phosphates
  作者：Daniel M. Lajoie、Pamela A. Zobel-Thropp、Vlad K. Kumirov、Vahe Bandarian、Greta J. Binford、Matthew H. J. Cordes

  DOI：10.1371/journal.pone.0072372

  日期：——

  Venoms of brown spiders in the genus Loxosceles contain phospholipase D enzyme toxins that can cause severe dermonecrosis and even death in humans. These toxins cleave the substrates sphingomyelin and lysophosphatidylcholine in mammalian tissues, releasing the choline head group. The other products of substrate cleavage have previously been reported to be monoester phospholipids, which would result from substrate hydrolysis. Using 31P NMR and mass spectrometry we demonstrate that recombinant toxins, as well as whole venoms from diverse Loxosceles species, exclusively catalyze transphosphatidylation rather than hydrolysis, forming cyclic phosphate products from both major substrates. Cyclic phosphates have vastly different biological properties from their monoester counterparts, and they may be relevant to the pathology of brown spider envenomation.

  Loxosceles属棕蜘蛛的毒液中含有磷脂酶D酶毒素，可导致严重皮肤坏死，甚至导致人类死亡。这些毒素会分解哺乳动物组织中的鞘氨醇和溶血磷脂酰胆碱，释放胆碱头基。此前有报道称，分解底物的其他产物是单酯磷脂，这是底物水解的结果。我们使用31P NMR和质谱技术证明，重组毒素以及来自不同Loxosceles物种的完整毒液仅催化转磷酸化，而不是水解，从两种主要底物形成环状磷酸盐产物。环状磷酸盐与单酯磷酸盐具有截然不同的生物特性，可能与棕蜘蛛毒液致病有关。
• KALLURY, KRISHNA M. R.;GHAEMMAGHAMI, VIDA;KRULL, ULRICH J.;THOMPSON, MICH+, ANAL. CHIM. ACTA, 225,(1989) N, C. 369-389
  作者：KALLURY, KRISHNA M. R.、GHAEMMAGHAMI, VIDA、KRULL, ULRICH J.、THOMPSON, MICH+

  DOI：——

  日期：——
• Secretory phospholipase A2-α from Arabidopsis thaliana: functional parameters and substrate preference
  作者：Johanna Mansfeld、Renate Ulbrich-Hofmann

  DOI：10.1016/j.chemphyslip.2007.07.001

  日期：2007.12

  The secretory phospholipase A(2)-alpha from Arabidopsis thaliana (AtsPLA(2)-alpha), being one of the first plant sPLA(2)s obtained in purified state, has been characterised with respect to substrate preference and optimum conditions of catalysis. The optima of pH, temperature, and calcium concentration were similar to the parameters of secretory PLA(2)s from animals. However, substrate preferences markedly differed. In contrast to pancreatic PLA(2)s, AtsPLA(2)-alpha preferred zwitterionic phospholipids, and showed lower activity toward anionic phospholipids. In substrates with two identical fatty acid chains, AtsPLA(2)-alpha showed optimum activity toward phospholipids with decanoyl groups. In substrates with palmitoyl groups in sn-1 position, acyl chains with higher degree of unsaturation in sn-2 position were preferred, excluding arachidonic acid, showing the evolutionary adaptation of the enzyme to substrate composition in plants. Km values for short chain phospholipids were comparable to sPLA(2)s from animals, whereas k(cat) values were much smaller and interfacial activation was less important. (C) 2007 Elsevier Ireland Ltd. All rights reserved.
• Variable Substrate Preference among Phospholipase D Toxins from Sicariid Spiders
  作者：Daniel M. Lajoie、Sue A. Roberts、Pamela A. Zobel-Thropp、Jared L. Delahaye、Vahe Bandarian、Greta J. Binford、Matthew H.J. Cordes

  DOI：10.1074/jbc.m115.636951

  日期：2015.4

  Venoms of the sicariid spiders contain phospholipase D enzyme toxins that can cause severe dermonecrosis and even death in humans. These enzymes convert sphingolipid and lysolipid substrates to cyclic phosphates by activating a hydroxyl nucleophile present in both classes of lipid. The most medically relevant substrates are thought to be sphingomyelin and/or lysophosphatidylcholine. To better understand the substrate preference of these toxins, we used P-31 NMR to compare the activity of three related but phylogenetically diverse sicariid toxins against a diverse panel of sphingolipid and lysolipid substrates. Two of the three showed significantly faster turnover of sphingolipids over lysolipids, and all three showed a strong preference for positively charged (choline and/or ethanolamine) over neutral (glycerol and serine) headgroups. Strikingly, however, the enzymes vary widely in their preference for choline, the headgroup of both sphingomyelin and lysophosphatidylcholine, versus ethanolamine. An enzyme from Sicarius terrosus showed a strong preference for ethanolamine overcholine, whereas two paralogous enzymes from Loxosceles arizonica either preferred choline or showed no significant preference. Intrigued by the novel substrate preference of the Sicarius enzyme, we solved its crystal structure at 2.1 angstrom resolution. The evolution of variable substrate specificity may help explain the reduced dermonecrotic potential of some natural toxin variants, because mammalian sphingolipids use primarily choline as a positively charged headgroup; it may also be relevant for sicariid predatory behavior, because ethanolamine-containing sphingolipids are common in insect prey.