peonidin-3-glucoside | 47729-58-8

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 黄酮类化合物
• 英文名称: peonidin-3-glucoside
• 英文别名: peonidin-3-O-glucoside；(3R,4S,5S,6R)-2-[5,7-dihydroxy-2-(4-hydroxy-3-methoxyphenyl)chromenylium-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 47729-58-8
• 化学式: C₂₂H₂₃O₁₁
• 分子量: 463.418
• InChiKey: ZZWPMFROUHHAKY-GDFBDPINSA-O

计算性质

• 辛醇/水分配系数(LogP)：
  0.69
• 重原子数：
  33
• 可旋转键数：
  5
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  170
• 氢给体数：
  7
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  cyanidin-3-O-glucoside 在 甲酸 、 1,3-双((三羟甲基)甲基氨基)丙烷 、 Vitis vinifera flavonol and anthocyanin O-methyltransferase 作用下， 以 水 为溶剂， 生成 peonidin-3-glucoside
  参考文献：
  名称：

  Characterization of a Vitis vinifera cv. Cabernet Sauvignon 3′,5′-O-methyltransferase showing strong preference for anthocyanins and glycosylated flavonols

  摘要：

  At ripening initiation in red grapevine (Vitis vinifera) berries, the exocarp turns color from green to red and then to purple due to the accumulation and extent of methylation of anthocyanins. The accumulation of transcripts encoding an O-methyltransferase was recently shown to be closely correlated with the onset of ripening and the degree of blue/purple pigmentation in grapevine berries; however, the biochemical function of this gene has remained uncharacterized. In this study, an O-methyltransferase cDNA that showed a distinct expression pattern when compared to closely related sequences was expressed in Escherichia coli and enzyme assays were carried out with a broad array of anthocyanin and other flavonoid substrates. We demonstrate that this enzyme carries out 3',5'-O-methylation of anthocyanins and flavonol compounds in vitro, which are known to be present in grape berries, with a preference for glycosylated substrates. The highest relative specific activity for the enzyme was found with delphinidin 3-O-glucoside as substrate. The enzyme is not able to methylate flavan type skeletons with chiral centers, such as either catechins or dihydroquercetin. The enzyme showed negligible specific activity for caffeoyl-CoA, compared to flavonol and anthocyanin substrates. Phylogenetic analysis of the O-methyltransferase suggests that it may be a member of a distinct subclass of Type 2 bivalent metal-dependent S-adenosylmethionine O-methyltransferases. Crown Copyright (C) 2010 Published by Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.phytochem.2010.05.027