erycibenins A

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 异黄酮类化合物
• 英文名称: erycibenins A
• 英文别名: 3,4-dihydro-3,5-dihydroxy-7-(4-hydroxyphenyl)-2,2-dimethyl-2H,6H-benzo[1,2-b:5,4-b']dipyran-6-one；3,5-Dihydroxy-7-(4-hydroxyphenyl)-2,2-dimethyl-3,4-dihydropyrano[3,2-g]chromen-6-one
• 化学式: C₂₀H₁₈O₆
• 分子量: 354.359
• InChiKey: WXQNEGHFLYKCJC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  26
• 可旋转键数：
  1
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  96.2
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  Wighteone; 5,7,4'三羟基-6-异戊烯基异黄酮 在 protein extract from Botrytis cinerea 、 还原型辅酶II(NADPH)四钠盐 作用下， 以 乙酸乙酯 为溶剂， 生成 ErythrininC;2,3-二氢-4-羟基-2-(1-羟基-1-甲基乙基)-6-(4-羟基苯基)-5H-呋喃并[3,2-g][1]苯并吡喃-5-酮 、 6-(2,3-Dihydroxy-3-methyl-butyl)-5,7-dihydroxy-3-(4-hydroxy-phenyl)-chromen-4-one 、 erycibenins A
  参考文献：
  名称：

  Fad-dependent epoxidase as a key enzyme in fungal metabolism of prenylated flavonoids

  摘要：

  Crude protein extracts from Botrytis cinerea preincubated with 6-prenylnaringenin (6-PN) for 20 hr catalysed the prenyl epoxidation of 7-O-methyl-luteone. The resulting epoxide was non-enzymatically and slowly converted into the corresponding dihydrofurano derivative in a buffer solution at pH 7.5. Preparation of cell-free extracts in the presence of 6-PN from the mycelia without preincubation with 6-PN hardly showed the epoxidizing activity. These facts revealed that the substrate analogue 6-PN has a role as an enzyme inducer rather than stabilizer. The enzyme reaction depends on molecular oxygen and NADPH. Low amounts of FAD were necessary for maximal enzyme activity. The enzymatic activity was not inhibited by various inhibitors of cytochrome P-450 tested, in addition to carbon monoxide and cytochrome c. The results indicated that this enzyme does not belong to the monooxygenases dependent on cytochrome P-450, but to those dependent on FAD. About half of. the total enzyme activity was found in the 125 000 g supernatant, but the specific activity for the epoxidation reaction in the 125 000 g pellet was 3.7-fold higher than in the soluble fraction. The enzyme showed high specificity to monoprenyl isoflavones. Finally, a preliminary experiment using a cell-free system from white lupin hypocotyls resulted in formation of small amounts of an epoxide corresponding to 7-O-methyl-luteone used as the substrate. (C) 1997 Elsevier Science Ltd.

  DOI：

  10.1016/s0031-9422(97)00322-1

文献信息

• Fad-dependent epoxidase as a key enzyme in fungal metabolism of prenylated flavonoids
  作者：Mitsuharu Tanaka、Satoshi Tahara

  DOI：10.1016/s0031-9422(97)00322-1

  日期：1997.10

  Crude protein extracts from Botrytis cinerea preincubated with 6-prenylnaringenin (6-PN) for 20 hr catalysed the prenyl epoxidation of 7-O-methyl-luteone. The resulting epoxide was non-enzymatically and slowly converted into the corresponding dihydrofurano derivative in a buffer solution at pH 7.5. Preparation of cell-free extracts in the presence of 6-PN from the mycelia without preincubation with 6-PN hardly showed the epoxidizing activity. These facts revealed that the substrate analogue 6-PN has a role as an enzyme inducer rather than stabilizer. The enzyme reaction depends on molecular oxygen and NADPH. Low amounts of FAD were necessary for maximal enzyme activity. The enzymatic activity was not inhibited by various inhibitors of cytochrome P-450 tested, in addition to carbon monoxide and cytochrome c. The results indicated that this enzyme does not belong to the monooxygenases dependent on cytochrome P-450, but to those dependent on FAD. About half of. the total enzyme activity was found in the 125 000 g supernatant, but the specific activity for the epoxidation reaction in the 125 000 g pellet was 3.7-fold higher than in the soluble fraction. The enzyme showed high specificity to monoprenyl isoflavones. Finally, a preliminary experiment using a cell-free system from white lupin hypocotyls resulted in formation of small amounts of an epoxide corresponding to 7-O-methyl-luteone used as the substrate. (C) 1997 Elsevier Science Ltd.