etoposide-β-glucoside | 135970-29-5

• 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: etoposide-β-glucoside
• CAS: 135970-29-5
• 化学式: C₃₅H₄₂O₁₈
• 分子量: 750.708
• InChiKey: CBWDUPOIICXZSK-QJTGLUQTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.19
• 重原子数：
  53.0
• 可旋转键数：
  8.0
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.63
• 拓扑面积：
  239.98
• 氢给体数：
  6.0
• 氢受体数：
  18.0

反应信息

• 作为产物：
  描述：

  尿苷(5')二氢二磷酰(1)-alpha-D-葡萄糖 、 依托泊苷 在 UDP-sugar glycosyltransferase 71C₁ 作用下， 生成 etoposide-β-glucoside
  参考文献：
  名称：

  Substrate specificities of family 1 UGTs gained by domain swapping

  摘要：

  Family 1 glycosyltransferases are a group of enzymes known to embrace a large range of different substrates. This study devises a method to enhance the range of substrates even further by combining domains from different glycosyltransferases to gain improved substrate specificity and catalytic efficiency. Chimeric glycosyltransferases were made by combining domains from seven different family 1 glycosyltransferases, UGT71C1, UGT71C2, UGT71E1, UGT85C1, UGT85B1, UGT88B1 and UGT94B1. Twenty different chimeric glycosyltransferases were formed of which twelve were shown to be catalytically active. The chimeric enzymes of Arabidopsis thaliana UGT71C1 and UGT71C2 showed major changes in acceptor substrate specificity and were able to glycosylate etoposide significantly better than the parental UGT71C1 and UGT71C2 enzymes, with K-cat and efficiency coefficients 3.0 and 2.6 times higher, respectively. Chimeric glycosyltransferases of UGT71C1 combined with Stevia rebaudiana UGT71E1, also afforded enzymes with high catalytic efficiency, even though the two enzymes only display 38% amino acid sequence identity. These chimeras show a significantly altered regiospecificity towards especially trans-resveratrol, enabling the production of trans-resveratrol-beta-4'-O-glucoside (resveratroloside). The study demonstrates that it is possible to obtain improved catalytic properties by combining domains from both closely as well as more distantly related glycosyltransferases. The substrate specificity gained by the chimeras is difficult to predict because factors determining the acceptor specificity reside in the N-terminal as well as the C-terminal domains. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.phytochem.2009.01.013