(-)-β-peltatin-A-methyl ether | 23978-65-6

• 分子结构分类: 有机化合物 - 木脂素、新木脂素和相关化合物 - 木脂素内酯
• 英文名称: (-)-β-peltatin-A-methyl ether
• 英文别名: β-peltatin A methyl ether；β-peltatin-A methyl ether；β-peltatin-A methylether；β-peltatin-a-methylether；β-peltatin-A-methyleter；O-Methyl-β-peltatin-A；beta-Peltatin A methyl ether；(5aR,8aR,9R)-4-methoxy-9-(3,4,5-trimethoxyphenyl)-5a,6,8a,9-tetrahydro-5H-[2]benzofuro[6,5-f][1,3]benzodioxol-8-one
• CAS: 23978-65-6
• 化学式: C₂₃H₂₄O₈
• 分子量: 428.439
• InChiKey: BFKORKXLSJUYSS-RQUSPXKASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  31
• 可旋转键数：
  5
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  81.7
• 氢给体数：
  0
• 氢受体数：
  8

反应信息

• 作为产物：
  描述：

  6,7-demethylenedeoxypodophyllotoxin 在 N-溴代丁二酰亚胺(NBS) 、 cesium fluoride 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 27.0h， 生成 (-)-β-peltatin-A-methyl ether
  参考文献：
  名称：

  Yamaguchi, Hideo; Nakajima, Syunji; Arimoto, Masao, Chemical and pharmaceutical bulletin, 1984, vol. 32, # 5, p. 1754 - 1760

  摘要：

  DOI：

文献信息

• TRANSGLUTAMINASE ACTIVATOR
  申请人：Kao Corporation

  公开号：EP2918280A1

  公开（公告）日：2015-09-16

  A transglutaminase activator containing at least one kind selected from the group consisting of an extract from Justicia procumbens, an extract from Peristrophe japonica, and a compound represented by Formula (1), as an active ingredient: wherein R1 and R2 represent a hydrogen atom, a hydroxyl group, or an alkoxy group having 1 to 4 carbon atoms; R3 represents a hydrogen atom, or a group for forming a methylenedioxy group by bonding with R2; R4 and R5 represent a hydrogen atom, or a group for forming a methylenedioxy group by bonding with each other; R6 represents a hydrogen atom, a hydroxyl group, an alkoxy group having 1 to 5 carbon atoms, an acyloxy group having 1 to 4 carbon atoms, or a specific sugar residue.

  一种转谷氨酰胺酶激活剂，其活性成分中至少含有一种从 Justicia procumbens 提取物、Peristrophe japonica 提取物和由式（1）代表的化合物组成的组中选出的物质： 其中 R1 和 R2 代表氢原子、羟基或具有 1 至 4 个碳原子的烷氧基；R3 代表氢原子或通过与 R2 键合形成亚甲二氧基的基团；R4 和 R5 代表氢原子或通过相互键合形成亚甲二氧基的基团；R6 代表氢原子、羟基、具有 1 至 5 个碳原子的烷氧基、具有 1 至 4 个碳原子的酰氧基或特定的糖残基。
• Components of Podophyllin. III. Isolation of α- and β-Peltatin. Structure Studies¹
  作者：Jonathan L. Hartwell、Wendell E. Detty

  DOI：10.1021/ja01157a068

  日期：1950.1
• Bartek et al., Collection of Czechoslovak Chemical Communications, 1956, vol. 21, p. 392,402, 403 Anm.
  作者：Bartek et al.

  DOI：——

  日期：——
• Components of Podophyllin. X.¹ Relation of α-Peltatin to β-Peltatin
  作者：Jonathan L. Hartwell、Anthony W. Schrecker、Gertrude Y. Greenberg

  DOI：10.1021/ja01144a512

  日期：1952.12
• Aryltetralin-lignan formation in two different cell suspension cultures of Linum album: Deoxypodophyllotoxin 6-hydroxylase, a key enzyme for the formation of 6-methoxypodophyllotoxin
  作者：Katja Federolf、A. Wilhelm Alfermann、Elisabeth Fuss

  DOI：10.1016/j.phytochem.2007.02.031

  日期：2007.5

  Suspension cultures initiated from two different Linum album seedlings accumulate either podophyllotoxin (PTOX, 2.6 mg/g DW) or 6-methoxypodophyllotoxin (6MPTOX, 5.4 mg/g DW) as main lignans. Two molecules of coniferyl alcohol are dimerized to pinoresinol which is converted via several steps into deoxypodophyllotoxin (DOP) which seems to be the branching point to PTOX or 6MPTOX biosynthesis. DOP is hydroxylated at position 7 to give PTOX by deoxypodophyllotoxin 7-hydroxylase (DOP7H). In contrast, 6MPTOX biosynthesis is achieved by DOP hydroxylation at position 6 to beta-peltatin by the cytochrome P450 enzyme deoxypodophyllotoxin 6-hydroxylase (DOP6H). The following methylation to beta-peltatin-A-methylether is catalyzed by beta-peltatin 6-O-methyltransferase (beta P6OMT) from which 6MPTOX is formed by hydroxylation at position 7 by beta-peltatin-A-methylether 7-hydroxylase (PAM7H). DOP6H and beta P6OMT could be characterized in protein extracts from cell cultures of L. flavum and L. nodiflorum, respectively, and here in L. album for the first time. DOP7H and PAM7H activities could not yet be detected with protein extracts. Experiments of feeding DOP together with inhibitors of cytochrome P450 depending as well as dioxygenase enzymes were performed in order to shed light on the type of DOP7H and PAM7H. Growth parameters and specific activities of enzymes from the phenylpropane as well as the lignan specific biosynthetic pathway were measured during a culture period of 16 days. From the enzymes studied only the DOP6H showed a differential activity sustaining the hypothesis that this enzyme is responsible for the differential lignan accumulation in both cell lines. (C) 2007 Elsevier Ltd. All rights reserved.