2,3-Dihexanoyl-sn-glycerol | 108648-10-8

• 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: 2,3-Dihexanoyl-sn-glycerol
• 英文别名: [(2R)-2-hexanoyloxy-3-hydroxypropyl] hexanoate
• CAS: 108648-10-8
• 化学式: C₁₅H₂₈O₅
• 分子量: 288.384
• InChiKey: DRUFTGMQJWWIOL-CYBMUJFWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  20
• 可旋转键数：
  14
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.87
• 拓扑面积：
  72.8
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  三己精 在 oat seed lipase 、 水 作用下， 反应 0.08h， 生成 1,2-二己酰-Sn-甘油 、 2,3-Dihexanoyl-sn-glycerol
  参考文献：
  名称：

  Positional Specificity and Stereoselectivity of a Lipase Preparation from Oat Seeds Acting on 1,2,3-Trihexanoylglycerol

  摘要：

  燕麦种子脂肪酶用含 0.5% Triton X-100 的 0.01 m 氯化钙溶液提取，并用硫酸铵沉淀。沉淀物溶解在 pH 值为 6.0 的磷酸盐缓冲液中，上清液用作脂肪酶制剂。这种脂肪酶对 1,2,3-三己酰甘油的酯位有很强的选择性，水解 Sn-3 的速度最快，水解 sn-1 的速度一般，水解 sn-2 的速度几乎为零。

  DOI：

  10.1271/bbb.61.166

文献信息

• Studies on the substrate specificity of purified human milk lipoprotein lipase
  作者：C. ‐S. Wang、A. Kuksis、F. Manganaro

  DOI：10.1007/bf02534942

  日期：1982.4

  The fatty acid specificity of purified human milk lipoprotein lipase was studied using the C₁₈ to C₅₄ (total acyl carbon number) saturated and the C₅₄ mono‐, di‐ and triunsaturated monoacid triacylglycerols. Kinetic determinations indicated that the medium‐chain triacylglycerols were better substrates than long‐ or very short‐chain saturated triacylglycerols. The unsaturated triacylglycerols were hydrolyzed at rates comparable to that of tricaprylin with triolein having the highest rate of hydrolysis of the unsaturated species tested. The enzyme attacked the primary ester bond much more readily than the secondary ester bond. The purified human milk lipoprotein lipase showed a preferential stereospecific lipolysis of thesn‐1‐position of the triacylglycerol molecule.

  摘要 使用 C18 至 C54（酰基总碳数）饱和和 C54 单酸、双酸和三酸三酰甘油研究了纯化人乳脂蛋白脂肪酶的脂肪酸特异性。动力学测定表明，与长链或极短链饱和三酰甘油相比，中链三酰甘油是更好的底物。不饱和三酰甘油的水解速度与三碳甘油酯的水解速度相当，其中三烯甘油酯的水解速度在所测试的不饱和三酰甘油酯中最高。该酶攻击一级酯键的速度比攻击二级酯键的速度快得多。纯化的人乳脂蛋白脂肪酶对三酰基甘油分子的sn-1位显示出优先的立体特异性脂肪分解作用。
• A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase
  作者：Thorsten Eggert、Gaëlle Pencreac‘h、Isabelle Douchet、Robert Verger、Karl-Erich Jaeger

  DOI：10.1046/j.1432-1327.2000.01736.x

  日期：2000.11

  A novel gene lipB, which encodes an extracellular lipolytic enzyme, was identified in the Bacillus subtilis genomic DNA sequence. We have cloned and overexpressed lipB in B. subtilis and Escherichia coli and have also purified the enzyme from a B. subtilis culture supernatant to electrophoretic homogeneity. Four different lipase assays were used to determine its catalytic activity: pH‐stat, spectrophotometry, fluorimetry and the monomolecular film technique. LipB preferentially hydrolysed triacylglycerol‐esters and p‐nitrophenyl‐esters of fatty acids with short chain lengths of ≤ 10 carbon atoms. Triolein, which is a typical substrate for true lipases, was not hydrolysed at all. These results led us to classify LipB as an esterase rather than a lipase. The catalytic triad of LipB consists of residues Ser78, Asp134, and His157 as demonstrated by amino‐acid sequence alignments and site‐directed mutagenesis. The nucleophile Ser78 is located in a lipase‐specific consensus sequence, which is Ala‐X‐Ser‐X‐Gly for most Bacillus lipases. All other bacterial lipases contain a glycine residue instead of the alanine at position‐2 with respect to the catalytic serine. We have investigated the role of this alanine residue by constructing LipB variant A76G, thereby restoring the lipase‐specific consensus motif. When compared with LipB this variant showed a markedly reduced thermostability but an increased stability at pH 5–7. Determination of the specific activities of wild‐type LipB and variant A76G using a monomolecular film of the substrate monoolein revealed an interesting result: the A76G substitution had converted the esterase LipB into a monoacylglycerol hydrolase.
• Positional Specificity and Stereoselectivity of a Lipase Preparation from Oat Seeds Acting on 1,2,3-Trihexanoylglycerol
  作者：Yasuhide Ota、Toshio Minesaki、Oshima Aki

  DOI：10.1271/bbb.61.166

  日期：1997.1

  Oat seed lipase was extracted with 0.01 m calcium chloride solution containing 0.5% Triton X-100 and precipitated with ammonium sulfate. The precipitate was dissolved in phosphate buffer at pH 6.0 and the supernatant was used as the lipase preparation. The lipase was very selective in the ester positions of 1,2,3-trihexanoylglycerol, hydrolyzing sn-3 most quickly, sn-1 moderately, and sn-2 hardly at all.

  燕麦种子脂肪酶用含 0.5% Triton X-100 的 0.01 m 氯化钙溶液提取，并用硫酸铵沉淀。沉淀物溶解在 pH 值为 6.0 的磷酸盐缓冲液中，上清液用作脂肪酶制剂。这种脂肪酶对 1,2,3-三己酰甘油的酯位有很强的选择性，水解 Sn-3 的速度最快，水解 sn-1 的速度一般，水解 sn-2 的速度几乎为零。