4-hydroxycinnamic alcohol 4-O-β-D-glucoside

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 4-hydroxycinnamic alcohol 4-O-β-D-glucoside
• 英文别名: p‐coumaryl alcohol glucoside；(2R,3S,4S,5R,6S)-2-(hydroxymethyl)-6-[4-(3-hydroxyprop-1-enyl)phenoxy]oxane-3,4,5-triol
• 化学式: C₁₅H₂₀O₇
• 分子量: 312.32
• InChiKey: CRVXJSNSTGEXDX-UXXRCYHCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  22
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  120
• 氢给体数：
  5
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  尿苷(5')二氢二磷酰(1)-alpha-D-葡萄糖 、 4-羟基肉桂醇 在 magnesium chloride 、 BSA 作用下， 以 二甲基亚砜 为溶剂， 生成 4-hydroxycinnamic alcohol 4-O-β-D-glucoside
  参考文献：
  名称：

  Oxidation of Monolignols by Members of the Berberine Bridge Enzyme Family Suggests a Role in Plant Cell Wall Metabolism

  摘要：

  Plant genomes contain a large number of genes encoding for berberine bridge enzyme (BBE)-like enzymes. Despite the wide-spread occurrence and abundance of this protein family in the plant kingdom, the biochemical function remains largely unexplored. In this study, we have expressed two members of the BBE-like enzyme family from Arabidopsis thaliana in the host organism Komagataella pastoris. The two proteins, termed AtBBE-like 13 and AtBBE-like 15, were purified, and their catalytic properties were determined. In addition, AtBBE-like 15 was crystallized and structurally characterized by x-ray crystallography. Here, we show that the enzymes catalyze the oxidation of aromatic allylic alcohols, such as coumaryl, sinapyl, and coniferyl alcohol, to the corresponding aldehydes and that AtBBE-like 15 adopts the same fold as vanillyl alcohol oxidase as reported previously for berberine bridge enzyme and other FAD-dependent oxidoreductases. Further analysis of the substrate range identified coniferin, the glycosylated storage form of coniferyl alcohol, as a substrate of the enzymes, whereas other glycosylated monolignols were rather poor substrates. A detailed analysis of the motifs present in the active sites of the BBE-like enzymes in A. thaliana suggested that 14 out of 28 members of the family might catalyze similar reactions. Based on these findings, we propose a novel role of BBE-like enzymes in monolignol metabolism that was previously not recognized for this enzyme family.

  DOI：

  10.1074/jbc.m115.659631