(25R)-spirost-5-en-3β-ol-O-α-L-rhmanopyranosyl-(1-2)-β-D-glucopyranoside | 390809-25-3

• 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: (25R)-spirost-5-en-3β-ol-O-α-L-rhmanopyranosyl-(1-2)-β-D-glucopyranoside
• 英文别名: (2S,3R,4R,5R,6S)-2-[(2R,3R,4S,5R,6R)-4,5-dihydroxy-6-(hydroxymethyl)-2-[(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-6-methyloxane-3,4,5-triol
• CAS: 390809-25-3
• 化学式: C₃₉H₆₂O₁₂
• 分子量: 722.914
• InChiKey: HDXIQHTUNGFJIC-DEMVPPTDSA-N

物化性质

• 沸点：
  838.8±65.0 °C(Predicted)
• 密度：
  1.34±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  51
• 可旋转键数：
  5
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.95
• 拓扑面积：
  177
• 氢给体数：
  6
• 氢受体数：
  12

反应信息

• 作为反应物：
  描述：

  (25R)-spirost-5-en-3β-ol-O-α-L-rhmanopyranosyl-(1-2)-β-D-glucopyranoside 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184.0 mg的产率得到diosgenin 3-O-β-D-galactopyranoside
  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

• 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.