p-nitrophenyl ferulate

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 肉桂酸及其衍生物
• 英文名称: p-nitrophenyl ferulate
• 英文别名: (4-Nitrophenyl) 3-(4-hydroxy-3-methoxyphenyl)prop-2-enoate
• 化学式: C₁₆H₁₃NO₆
• 分子量: 315.282
• InChiKey: VIQDYVAKUJDZBD-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  23
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.06
• 拓扑面积：
  102
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  p-nitrophenyl ferulate 在 recombinant Aspergillus usamii E₀₀₁ type A feruloyl esterase 作用下， 以 aq. phosphate buffer 、 二甲基亚砜 为溶剂， 反应 0.17h， 生成 对硝基苯酚
  参考文献：
  名称：

  Contribution of Disulfide Bridges to the Thermostability of a Type A Feruloyl Esterase from Aspergillus usamii

  摘要：

  通过引入额外的二硫键或消除该酶的一个天然二硫键，研究了来自Aspergillus usamii E001的A型阿魏酯酶（AuFaeA）二硫桥对热稳定性的贡献。使用两种计算工具MODIP和DbD，可以预测蛋白质中可能的二硫桥以提高热稳定性，同时进行了分子动力学（MD）模拟，以设计额外的二硫桥。选择了一个残基对A126-N152，并将相应的氨基酸残基突变为半胱氨酸。在毕赤酵母GS115中表达了野生型AuFaeA及其变体。重组的(re-)AuFaeAA126C-N152C的最佳温度比re-AuFaeA提高了6°C。在55°C和60°C下，re-AuFaeAA126C-N152C的热失活半衰期分别为188分钟和40分钟，分别是re-AuFaeA的12.5倍和10倍。re-AuFaeAA126C-N152C的催化效率（kcat/Km）与re-AuFaeA相似。此外，在AuFaeA中消除每个天然二硫桥后，重组AuEaeA变体的表达水平大幅下降，热稳定性至少下降了10°C。

  DOI：

  10.1371/journal.pone.0126864
• 作为产物：
  描述：

  阿魏酸 在 4-二甲氨基吡啶 、 四丁基氟化铵 、 水 、 potassium carbonate 、 溶剂黄146 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 反应 21.5h， 生成 p-nitrophenyl ferulate
  参考文献：
  名称：

  四氢呋喃木质素的生物启发全合成

  摘要：

  木质素天然产物包含广泛的生物活性次生代谢产物。它们的结构多样性掩盖了常见的生物合成过程，其中涉及丙烯基酚的区域和化学选择性氧化偶联。复制这种氧化偶合的尝试已经揭示了控制选择性的重大挑战，并且迄今为止，这些挑战阻止了向木脂素家族化合物的统一仿生途径的发展。提出了一种实用的解决方案，该解决方案取决于二芳基环丁烷的氧化开环，以拦截假定的生物合成中间体。该方法的有效性通过从阿魏酸开始的4个步骤中的第一批全合成tanegool以及原型呋喃酮聚糖松脂醇的简明合成得到了证明。

  DOI：

  10.1002/anie.201408641

文献信息

• Purification and Characterization of Ferulic Acid Esterase from Malted Finger Millet (<i>Eleusine coracana</i>, Indaf-15)
  作者：G. Madhavi Latha、P. Srinivas、G. Muralikrishna

  DOI：10.1021/jf071918d

  日期：2007.11.1

  Ferulic acid esterase (EC 3.1.1.73) cleaves the feruloyl groups substituted at the 5'-OH group of arabinosyl residues of arabinoxylans and is known to modulate their functional properties. In this study, ferulic acid esterase from 96 h finger millet malt was purified to apparent homogeneity by three-step purification with a recovery of 3% and a fold purification of 22. The substrate p-nitrophenylferulate (PNPF) was synthesized and used to assay this enzyme spectrophotometrically. The products liberated from ragi and wheat water-soluble polysaccharides by the action of purified ragi ferulic acid esterase were identified by ESI-MS. The pH and temperature optima of the enzyme were found to be 6.0 and 45 degrees C, respectively. The pH and temperature stabilities of the enzyme were found to be in the range of 5.5-9.0 and 30 degrees C, respectively. The activation energy of the enzymatic reaction was found to be 4.08 kJ mol(-1). The apparent Km and V-max of the purified ferulic acid esterase for PNPF were 0.053 mu M and 0.085 unit mL(-1), respectively. The enzyme is a monomer with a molecular mass of 16.5 kDa. Metal ions such as Ni2+, Zn2+, Co2+, and Cu2+ and oxalic and citric acids enhanced the enzyme activity. The enzyme was completely inhibited by Fe3+. Group specific reagents such as p-chloromercuric benzoate and iodoacetamide inhibited the enzyme, indicating the possible presence of cysteine residues in the active site pocket.
• A Bio-Inspired Total Synthesis of Tetrahydrofuran Lignans
  作者：Anna K. F. Albertson、Jean-Philip Lumb

  DOI：10.1002/anie.201408641

  日期：2015.2.9

  unified biomimetic route to compounds of the lignan family. A practical solution is presented that hinges on oxidative ring opening of a diarylcyclobutane to intercept a putative biosynthetic intermediate. The effectiveness of this approach is demonstrated by the first total synthesis of tanegool in 4 steps starting from ferulic acid, as well as a concise synthesis of the prototypical furanolignan pinoresinol

  木质素天然产物包含广泛的生物活性次生代谢产物。它们的结构多样性掩盖了常见的生物合成过程，其中涉及丙烯基酚的区域和化学选择性氧化偶联。复制这种氧化偶合的尝试已经揭示了控制选择性的重大挑战，并且迄今为止，这些挑战阻止了向木脂素家族化合物的统一仿生途径的发展。提出了一种实用的解决方案，该解决方案取决于二芳基环丁烷的氧化开环，以拦截假定的生物合成中间体。该方法的有效性通过从阿魏酸开始的4个步骤中的第一批全合成tanegool以及原型呋喃酮聚糖松脂醇的简明合成得到了证明。
• Contribution of Disulfide Bridges to the Thermostability of a Type A Feruloyl Esterase from Aspergillus usamii
  作者：Xin Yin、Die Hu、Jian-Fang Li、Yao He、Tian-Di Zhu、Min-Chen Wu

  DOI：10.1371/journal.pone.0126864

  日期：——

  The contribution of disulfide bridges to the thermostability of a type A feruloyl esterase (AuFaeA) from Aspergillus usamii E001 was studied by introducing an extra disulfide bridge or eliminating a native one from the enzyme. MODIP and DbD, two computational tools that can predict the possible disulfide bridges in proteins for thermostability improvement, and molecular dynamics (MD) simulations were used to design the extra disulfide bridge. One residue pair A126-N152 was chosen, and the respective amino acid residues were mutated to cysteine. The wild-type AuFaeA and its variants were expressed in Pichia pastoris GS115. The temperature optimum of the recombinant (re-) AuFaeAA126C-N152C was increased by 6°C compared to that of re-AuFaeA. The thermal inactivation half-lives of re-AuFaeAA126C-N152C at 55 and 60°C were 188 and 40 min, which were 12.5- and 10-folds longer than those of re-AuFaeA. The catalytic efficiency (kcat/Km) of re-AuFaeAA126C-N152C was similar to that of re-AuFaeA. Additionally, after elimination of each native disulfide bridge in AuFaeA, a great decrease in expression level and at least 10°C decrease in thermal stability of recombinant AuEaeA variants were also observed.

  通过引入额外的二硫键或消除该酶的一个天然二硫键，研究了来自Aspergillus usamii E001的A型阿魏酯酶（AuFaeA）二硫桥对热稳定性的贡献。使用两种计算工具MODIP和DbD，可以预测蛋白质中可能的二硫桥以提高热稳定性，同时进行了分子动力学（MD）模拟，以设计额外的二硫桥。选择了一个残基对A126-N152，并将相应的氨基酸残基突变为半胱氨酸。在毕赤酵母GS115中表达了野生型AuFaeA及其变体。重组的(re-)AuFaeAA126C-N152C的最佳温度比re-AuFaeA提高了6°C。在55°C和60°C下，re-AuFaeAA126C-N152C的热失活半衰期分别为188分钟和40分钟，分别是re-AuFaeA的12.5倍和10倍。re-AuFaeAA126C-N152C的催化效率（kcat/Km）与re-AuFaeA相似。此外，在AuFaeA中消除每个天然二硫桥后，重组AuEaeA变体的表达水平大幅下降，热稳定性至少下降了10°C。