diosgenin 3-O-α-L-rhamnopyranosyl(1->4)-α-L-rhamnopyranosyl(1->4)-β-D-glucopyranoside

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 类固醇和类固醇衍生物
• 英文名称: diosgenin 3-O-α-L-rhamnopyranosyl(1->4)-α-L-rhamnopyranosyl(1->4)-β-D-glucopyranoside
• 英文别名: diosgenyl α-L-rhamnopyranosyl-(1->4)-α-L-rhamnopyranosyl-(1->4)-β-D-glucopyranoside；(25R*)-spirost-5-en-3β-yl α-L-rhamnopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→4)-β-D-glucopyranoside；(2S,3R,4R,5R,6S)-2-[(2S,3R,4S,5R,6S)-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(1S,2S,4S,5'R,6R,7S,8R,9S,12S,13R,16S)-5',7,9,13-tetramethylspiro[5-oxapentacyclo[10.8.0.02,9.04,8.013,18]icos-18-ene-6,2'-oxane]-16-yl]oxyoxan-3-yl]oxy-4,5-dihydroxy-2-methyloxan-3-yl]oxy-6-methyloxane-3,4,5-triol
• 化学式: C₄₅H₇₂O₁₆
• 分子量: 869.057
• InChiKey: CLBAIZZJADAEOT-ZVWYDXNDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  61
• 可旋转键数：
  7
• 环数：
  9.0
• sp3杂化的碳原子比例：
  0.96
• 拓扑面积：
  236
• 氢给体数：
  8
• 氢受体数：
  16

反应信息

• 作为产物：
  描述：

  重楼皂苷B 在 Curvularia lunata 3.4381 1,4-α-D-glucan glucohydrolase 作用下， 以 phosphate buffer 为溶剂， 反应 6.0h， 以31.0 mg的产率得到diosgenin 3-O-α-L-rhamnopyranosyl(1->4)-α-L-rhamnopyranosyl(1->4)-β-D-glucopyranoside
  参考文献：
  名称：

  The substrate specificity of a glucoamylase with steroidal saponin-rhamnosidase activity from Curvularia lunata

  摘要：

  In previous work, we studied and reported that an enzyme from Curvularia lunata 3.4381 had the novel specificity to hydrolyze the terminal rhamnosyl at C-3 position of steroidal saponin and obtained four transformed products; the enzyme was purified and ascertained as glucoamylase (EC 3.2.1.3 GA). In this work, the enzyme exhibiting steroidal saponin-rhamnosidase activity was systematically studied on 21 steroidal saponins and 6 ginsenosides. The results showed that the alpha-1,2-linked end-rhamnosyl residues at C-3 position of steroidal saponins could be hydrolyzed to corresponding secondary steroidal saponins, among which 18 compounds were isolated and identified, including 3 new secondary compounds. For the furostanosides having glucosyl residues at the C-26 position, hydrolysis occurred first at end- rhamnosyl at C-3 position to produce secondary furostanosides. The reaction of hydrolyzing glucosyl at C-26 position depended considerably on longer reaction times yielding the corresponding secondary spirostanosides ( without rhamnosyl and glucosyl residues). The enzyme had the strict specificity for the terminal alpha-1,2-linked rhamnosyl residues of linear chain, or the terminal alpha-1,2-linked rhamnosyl residues with branched chain of 1,4-linked glycosyl residues of sugar chain at C-3 position of steroidal saponins, it was not specific for different aglycones, different glycons, and the number of glycon of sugar chain of steroidal saponin. The end- rhamnosyl of ginsenosides and p-nitrophenyl-a-L-rhamnopyranoside (pNPR) could not be hydrolyzed by the enzyme from C. lunata. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2007.04.076

文献信息

• Synthesis of a group of diosgenyl saponins with combined use of glycosyl trichloroacetimidate and thioglycoside donors
  作者：Hai Yu、Biao Yu、Xiangyang Wu、Yongzheng Hui、Xiuwen Han

  DOI：10.1039/a909218h

  日期：——

  With the combined use of glycosyl trichloroacetimidates and thioglycosides, a group of natural diosgenyl saponins (1–6) are efficiently synthesized, in either a stepwise or a ‘one-pot’ manner. The trichloroacetimidate is employed as an efficient temporary hydroxy protecting group in glycosylation with the glycosyl trichloroacetimidate. The intermolecular alkylthio-group transfer is demonstrated to be a common side-reaction during glycosylation with thioglycosides.

  通过结合使用糖基三氯乙亚胺酯和硫代糖苷，一系列天然薯蓣皂苷元的皂苷（1-6）被高效地合成，无论是逐步合成还是“一锅法”合成。三氯乙亚胺酯作为糖基化反应中糖基三氯乙亚胺酯的临时羟基保护组，表现出高效性。硫代糖苷参与的糖基化反应中，分子的烷硫基转移被证实是一种常见的副反应。
• Synthesis of a group of diosgenyl saponins by a one-pot sequential glycosylation
  作者：Biao Yu、Hai Yu、Yongzheng Hui、Xiuwen Han

  DOI：10.1016/s0040-4039(99)01839-0

  日期：1999.12

  A group of natural diosgenyl saponins was synthesized in a highly efficient manner employing the 'one-pot sequential glycosylation' protocol with the combined use of glycosyl trichloroacetimidates and thioglycosides. (C) 1999 Elsevier Science Ltd. All rights reserved.
• The substrate specificity of a glucoamylase with steroidal saponin-rhamnosidase activity from Curvularia lunata
  作者：Bing Feng、Li-ping Kang、Bai-ping Ma、Bo Quan、Wen-bin Zhou、Yong-ze Wang、Yu Zhao、Yi-xun Liu、Sheng-qi Wang

  DOI：10.1016/j.tet.2007.04.076

  日期：2007.7

  In previous work, we studied and reported that an enzyme from Curvularia lunata 3.4381 had the novel specificity to hydrolyze the terminal rhamnosyl at C-3 position of steroidal saponin and obtained four transformed products; the enzyme was purified and ascertained as glucoamylase (EC 3.2.1.3 GA). In this work, the enzyme exhibiting steroidal saponin-rhamnosidase activity was systematically studied on 21 steroidal saponins and 6 ginsenosides. The results showed that the alpha-1,2-linked end-rhamnosyl residues at C-3 position of steroidal saponins could be hydrolyzed to corresponding secondary steroidal saponins, among which 18 compounds were isolated and identified, including 3 new secondary compounds. For the furostanosides having glucosyl residues at the C-26 position, hydrolysis occurred first at end- rhamnosyl at C-3 position to produce secondary furostanosides. The reaction of hydrolyzing glucosyl at C-26 position depended considerably on longer reaction times yielding the corresponding secondary spirostanosides ( without rhamnosyl and glucosyl residues). The enzyme had the strict specificity for the terminal alpha-1,2-linked rhamnosyl residues of linear chain, or the terminal alpha-1,2-linked rhamnosyl residues with branched chain of 1,4-linked glycosyl residues of sugar chain at C-3 position of steroidal saponins, it was not specific for different aglycones, different glycons, and the number of glycon of sugar chain of steroidal saponin. The end- rhamnosyl of ginsenosides and p-nitrophenyl-a-L-rhamnopyranoside (pNPR) could not be hydrolyzed by the enzyme from C. lunata. (c) 2007 Elsevier Ltd. All rights reserved.