D-α-Stearoyl-β-oleoylglycerin | 134731-52-5

• 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: D-α-Stearoyl-β-oleoylglycerin
• 英文别名: 2-Oleoyl-3-stearoyl-sn-glycerol；[(2R)-3-hydroxy-2-[(Z)-octadec-9-enoyl]oxypropyl] octadecanoate
• CAS: 134731-52-5
• 化学式: C₃₉H₇₄O₅
• 分子量: 623.014
• InChiKey: SAEPUUXWQQNLGN-XZRWTQCASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  15.3
• 重原子数：
  44
• 可旋转键数：
  37
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.9
• 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：

  D-α-Stearoyl-β-oleoylglycerin 、 Acetic acid (1R,2S,3S,4R,5R,6S)-2,3,4,5-tetraacetoxy-6-phosphonooxy-cyclohexyl ester 在 吡啶 、 2,4,6-三甲基苯磺酰氯 作用下， 生成 (Z)-Octadec-9-enoic acid (S)-2-[hydroxy-((1S,2R,3R,4S,5S,6R)-2,3,4,5,6-pentaacetoxy-cyclohexyloxy)-phosphoryloxy]-1-octadecanoyloxymethyl-ethyl ester
  参考文献：
  名称：

  Lyutik,A.I. et al., Journal of general chemistry of the USSR, 1974, vol. 44, p. 2559

  摘要：

  DOI：
• 作为产物：
  描述：

  Stearooleopalmitin 、 水 生成 D-α-Stearoyl-β-oleoylglycerin 、 氢(+1)阳离子 、 十六烷酸酯
  参考文献：
  名称：

  Purification and Characterization of a Catalytic Domain of Rat Intestinal Phospholipase B/Lipase Associated with Brush Border Membranes

  摘要：

  A brush border membrane-associated phospholipase B/lipase was solubilized from the distal two-thirds of rat small intestine by autolysis during storage at -35 degrees C over 1 month, and then the enzyme was purified to homogeneity and characterized enzymatically and structurally, The purified enzyme exhibited broad substrate specificity including esterase, phospholipase A(2), lysophospholipase, and lipase activities. SDS-gel electrophoretic and reverse-phase high performance liquid chromatographic analyses demonstrated that a single enzyme catalyzes these activities. It preferred hydrolysis at the sn-2 position of diacylphospholipid and diacylglycerol without strict stereoselectivity, whereas it apparently exhibited no positional specificity toward triacylglycerol. Diisopropyl fluorophosphate, an irreversible inhibitor of serine esterases and lipases, inhibited purified enzyme, When the position of enzyme on SDS-gel electrophoresis under the non-reducing conditions was determined by assaying the activity eluted from sliced gels, brush border membrane-associated enzyme corresponded to a similar to 150-kDa protein; autolysis gave a 35-kDa product, in agreement with the results of immunoblot analysis, The purified 35-kDa enzyme consisted of a 14-kDa peptide and a glycosylated 21-kDa peptide. Their NH2-terminal amino acid sequences were determined and found in the second repeat of 161-kDa phospholipase B/lipase with 4-fold tandem repeats of similar to 38 kDa each, which we cloned and sequenced in the accompanying paper (Takemori, H., Zolotaryov, F,, Ting, L., Urbain, T,, Komatsubara, T., Hatano, O., Okamoto, M,, and Tojo, H. (1998) J. Biol. Chem. 273, 2222-2231). These results indicate that the purified enzyme is the catalytic domain derived from the second repeat of brush border membrane-associated phospholipase B/lipase.

  DOI：

  10.1074/jbc.273.4.2214

文献信息

• Lyutik,A.I. et al., Journal of general chemistry of the USSR, 1974, vol. 44, p. 2559
  作者：Lyutik,A.I. et al.

  DOI：——

  日期：——
• Purification and Characterization of a Catalytic Domain of Rat Intestinal Phospholipase B/Lipase Associated with Brush Border Membranes
  作者：Hiromasa Tojo、Tetsuichi Ichida、Mitsuhiro Okamoto

  DOI：10.1074/jbc.273.4.2214

  日期：1998.1

  A brush border membrane-associated phospholipase B/lipase was solubilized from the distal two-thirds of rat small intestine by autolysis during storage at -35 degrees C over 1 month, and then the enzyme was purified to homogeneity and characterized enzymatically and structurally, The purified enzyme exhibited broad substrate specificity including esterase, phospholipase A(2), lysophospholipase, and lipase activities. SDS-gel electrophoretic and reverse-phase high performance liquid chromatographic analyses demonstrated that a single enzyme catalyzes these activities. It preferred hydrolysis at the sn-2 position of diacylphospholipid and diacylglycerol without strict stereoselectivity, whereas it apparently exhibited no positional specificity toward triacylglycerol. Diisopropyl fluorophosphate, an irreversible inhibitor of serine esterases and lipases, inhibited purified enzyme, When the position of enzyme on SDS-gel electrophoresis under the non-reducing conditions was determined by assaying the activity eluted from sliced gels, brush border membrane-associated enzyme corresponded to a similar to 150-kDa protein; autolysis gave a 35-kDa product, in agreement with the results of immunoblot analysis, The purified 35-kDa enzyme consisted of a 14-kDa peptide and a glycosylated 21-kDa peptide. Their NH2-terminal amino acid sequences were determined and found in the second repeat of 161-kDa phospholipase B/lipase with 4-fold tandem repeats of similar to 38 kDa each, which we cloned and sequenced in the accompanying paper (Takemori, H., Zolotaryov, F,, Ting, L., Urbain, T,, Komatsubara, T., Hatano, O., Okamoto, M,, and Tojo, H. (1998) J. Biol. Chem. 273, 2222-2231). These results indicate that the purified enzyme is the catalytic domain derived from the second repeat of brush border membrane-associated phospholipase B/lipase.