quercetin 7,4'-diglucoside

• 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: quercetin 7,4'-diglucoside
• 英文别名: 3,5-Dihydroxy-2-(3-hydroxy-4-(((3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)oxy)phenyl)-7-(((3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)tetrahydro-2H-pyran-2-yl)oxy)-4H-chromen-4-one；3,5-dihydroxy-2-[3-hydroxy-4-[(3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyphenyl]-7-[(3R,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxychromen-4-one
• 化学式: C₂₇H₃₀O₁₇
• 分子量: 626.525
• InChiKey: QZXHFNCQMMUANB-XOZSVDQDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.4
• 重原子数：
  44
• 可旋转键数：
  7
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  286
• 氢给体数：
  11
• 氢受体数：
  17

反应信息

• 作为产物：
  描述：

  尿苷(5')二氢二磷酰(1)-alpha-D-葡萄糖 、 槲皮素 在 phosphate buffer 作用下， 反应 0.5h， 生成 槲皮素 3'-β-D-葡萄糖苷 、 quercetin-4′-O-monoglucoside 、 quercetin-7-O-glucopyranoside 、 quercetin 7,4'-diglucoside
  参考文献：
  名称：

  Cloning and functional characterisation of two regioselective flavonoid glucosyltransferases from Beta vulgaris

  摘要：

  Two full-length cDNAs encoding flavonoid-specific glucosyltransferases, UGT73A4 and UGT71F1, were isolated from a cDNA library of Beta vulgaris (Amaranthaceac) cell suspension cultures. They displayed high identity to position-specific betanidin and flavonoid glucosyltransferases from Dorotheanthus bellidiformis (Aizoaceae) and to enzymes with similar substrate specificities from various plant families. The open reading frame of the sequences encode proteins of 476 (UGT73A4) and 492 (UGT71F1) amino acids with calculated molecular masses of 54.07 kDa and 54.39 kDa, and isoelectric points of 5.8 and 5.6, respectively. Both enzymes were functionally expressed in Escherichia coli as His- and GST-tagged proteins, respectively. They exhibited a broad substrate specificity, but a distinct regioselectivity, glucosylating a variety of flavonols, flavones, flavanones, and coumarins. UGT73A4 showed a preference for the 4'- and 7-OH position in the flavonoids, whereas UGT71F1 preferentially glucosylated the 3- or the 7-OH position. Glucosylation of betanidin, the aglycone of the major betacyanin, betanin, in B. vulgaris was also observed to a low extent by both enzymes. Several O-glycosylated vitexin derivatives isolated from leaves of young B. vulgaris plants and rutin obtained from B. vulgaris tissue culture are discussed as potential endogenous products of UGT73A4 and UGT71F1. The results are analyzed with regard to evolution and specificity of plant natural product glucosyltransferases., (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.phytochem.2006.06.026

文献信息

• [EN] PROCESS FOR PREPARING A BIOACTIVE FRACTION FROM RED ONION<br/>[FR] PROCÉDÉ DE PRÉPARATION D'UNE FRACTION BIOACTIVE ISSUE DE L'OIGNON ROUGE
  申请人：COUNCIL SCIENT IND RES

  公开号：WO2009141834A2

  公开（公告）日：2009-11-26

  The present invention deals with a process of preparing quercetin enriched and microencapsulated flavored bioactive fraction from red onion (Allium cepa L), wich possesses significant antioxidant and chelation properties. The present invention further deals with a process for commercial dewatering of onion for the preparation of microencapsulated flavored bioactive fraction from red onion (Allium cepa L).
• Cloning and functional characterisation of two regioselective flavonoid glucosyltransferases from Beta vulgaris
  作者：Judith Isayenkova、Victor Wray、Manfred Nimtz、Dieter Strack、Thomas Vogt

  DOI：10.1016/j.phytochem.2006.06.026

  日期：2006.8

  Two full-length cDNAs encoding flavonoid-specific glucosyltransferases, UGT73A4 and UGT71F1, were isolated from a cDNA library of Beta vulgaris (Amaranthaceac) cell suspension cultures. They displayed high identity to position-specific betanidin and flavonoid glucosyltransferases from Dorotheanthus bellidiformis (Aizoaceae) and to enzymes with similar substrate specificities from various plant families. The open reading frame of the sequences encode proteins of 476 (UGT73A4) and 492 (UGT71F1) amino acids with calculated molecular masses of 54.07 kDa and 54.39 kDa, and isoelectric points of 5.8 and 5.6, respectively. Both enzymes were functionally expressed in Escherichia coli as His- and GST-tagged proteins, respectively. They exhibited a broad substrate specificity, but a distinct regioselectivity, glucosylating a variety of flavonols, flavones, flavanones, and coumarins. UGT73A4 showed a preference for the 4'- and 7-OH position in the flavonoids, whereas UGT71F1 preferentially glucosylated the 3- or the 7-OH position. Glucosylation of betanidin, the aglycone of the major betacyanin, betanin, in B. vulgaris was also observed to a low extent by both enzymes. Several O-glycosylated vitexin derivatives isolated from leaves of young B. vulgaris plants and rutin obtained from B. vulgaris tissue culture are discussed as potential endogenous products of UGT73A4 and UGT71F1. The results are analyzed with regard to evolution and specificity of plant natural product glucosyltransferases., (c) 2006 Elsevier Ltd. All rights reserved.