dihydro-5-hydroxyconiferyl aldehyde | 863781-14-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 酚类
• 英文名称: dihydro-5-hydroxyconiferyl aldehyde
• 英文别名: 3-(3,4-Dihydroxy-5-methoxyphenyl)propanal；3-(3,4-dihydroxy-5-methoxyphenyl)propanal
• CAS: 863781-14-0
• 化学式: C₁₀H₁₂O₄
• 分子量: 196.203
• InChiKey: ILKRAECJLSFVDF-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.9
• 重原子数：
  14
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  66.8
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  5-hydroxyconiferyl aldehyde 在 Plagiochasma appendiculatum alkenal double bond reductase 2 、 还原型辅酶II(NADPH)四钠盐 作用下， 以 aq. phosphate buffer 为溶剂， 反应 0.5h， 生成 dihydro-5-hydroxyconiferyl aldehyde
  参考文献：
  名称：

  A single amino acid determines the catalytic efficiency of two alkenal double bond reductases produced by the liverwortPlagiochasma appendiculatum

  摘要：

  Alkenal double bond reductases (DBRs) catalyze the NADPH‐dependent reduction of the α,β‐unsaturated double bond of many secondary metabolites. Two alkenal double bond reductase genes PaDBR1 and PaDBR2 were isolated from the liverwort species Plagiochasma appendiculatum. Recombinant PaDBR2 protein had a higher catalytic activity than PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes. The residue at position 56 appeared to be responsible for this difference in enzyme activity. The functionality of a C56 to Y56 mutation in PaDBR1 was similar to that of PaDBR2. Further site‐directed mutagenesis and structural modeling suggested that the phenol ring stacking between this residue and the substrate was an important determinant of catalytic efficiency.

  DOI：

  10.1016/j.febslet.2013.07.051

文献信息

• A single amino acid determines the catalytic efficiency of two alkenal double bond reductases produced by the liverwort<i>Plagiochasma appendiculatum</i>
  作者：Yifeng Wu、Yuanheng Cai、Yi Sun、Ruixue Xu、Haina Yu、Xiaojuan Han、Hongxiang Lou、Aixia Cheng

  DOI：10.1016/j.febslet.2013.07.051

  日期：2013.9.17

  Alkenal double bond reductases (DBRs) catalyze the NADPH‐dependent reduction of the α,β‐unsaturated double bond of many secondary metabolites. Two alkenal double bond reductase genes PaDBR1 and PaDBR2 were isolated from the liverwort species Plagiochasma appendiculatum. Recombinant PaDBR2 protein had a higher catalytic activity than PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes. The residue at position 56 appeared to be responsible for this difference in enzyme activity. The functionality of a C56 to Y56 mutation in PaDBR1 was similar to that of PaDBR2. Further site‐directed mutagenesis and structural modeling suggested that the phenol ring stacking between this residue and the substrate was an important determinant of catalytic efficiency.