dTDP-vicenisamine | 852540-74-0

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘧啶核苷酸
• 英文名称: dTDP-vicenisamine
• CAS: 852540-74-0
• 化学式: C₁₇H₂₉N₃O₁₃P₂
• 分子量: 545.377
• InChiKey: SEPRQBOZGPJQKW-IKIFBEIWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.17
• 重原子数：
  35.0
• 可旋转键数：
  9.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.76
• 拓扑面积：
  228.1
• 氢给体数：
  6.0
• 氢受体数：
  13.0

反应信息

• 作为反应物：
  描述：

  dTDP-vicenisamine 、 Β-玉米赤霉烯醇 在 三羟甲基氨基甲烷盐酸盐 作用下， 以 二甲基亚砜 为溶剂， 反应 16.0h， 以9%的产率得到6'-O-vicenisaminyl-β-zearalenol
  参考文献：
  名称：

  Enzymatic Approach to Unnatural Glycosides with Diverse Aglycon Scaffolds Using Glycosyltransferase VinC

  摘要：

  Glycosyltransferase VinC was explored for a construction of glycoside libraries using dTDP-vicenisamine and structurally unrelated unnatural aglycons, and new unnatural vicenisaminides were successfully constructed. Structural elements of aglycon recognition by VinC were proposed by modeling studies and were confirmed by the success of transglycosylation upon a designed aglycon.

  DOI：

  10.1021/ja042848j
• 作为产物：
  描述：

  N-benzyloxycarbonyl-4-methylamino-2,4,6-trideoxy-D-ribo-hexopyranose 在 palladium on activated charcoal 氢气 作用下， 以 甲醇 、 水 为溶剂， 反应 2.5h， 生成 dTDP-vicenisamine
  参考文献：
  名称：

  Substrate Flexibility of Vicenisaminyltransferase VinC Involved in the Biosynthesis of Vicenistatin

  摘要：

  A glycosyltransferase VinC is involved in the biosynthesis of antitumor beta-glycoside antibiotic vicenistatin. It catalyzes a glycosyl transfer reaction between dTDP-alpha-D-vicenisamine and vicenilactam. Previous identification of its broad substrate specificity toward various glycosyl acceptors enabled us to explore the potential of VinC for glycodiversification. In vitro study of the substrate specificity toward several dTDP-sugars with vicenilactam established that VinC displayed activities with alpha-anomers of several dTDP-2-deoxy-D-sugars such as mycarose, digitoxose, olivose, and 2-deoxyglucose to afford respective beta-glycosides. Notably, beta-anomers of dTDP-2-deoxy-D-sugars also appeared to be accepted by VinC to form alpha-glycosides. Furthermore, VinC is capable of catalyzing glycosyl transfer reactions from both the alpha-anomer and beta-anomer of dTDP-L-mycarose, respectively, into beta-glycoside and alpha-glycoside. These results indicate that VinC is a unique glycosyltransferase possessing broad substrate specificity. The mechanism of this axially oriented glycosidic bond formation from the equatorially oriented dTDP-sugar might be explained by conformational change of dTDP-sugar to a boat conformation during the glycosyl transfer reaction. To apply these features of VinC for glycodiversification, 22 sets of structurally diverse glycosides were constructed using unnatural glycosyl donors and acceptors.

  DOI：

  10.1021/ja0685250

文献信息

• Aglycon switch approach toward unnatural glycosides from natural glycoside with glycosyltransferase VinC
  作者：Atsushi Minami、Katsumi Kakinuma、Tadashi Eguchi

  DOI：10.1016/j.tetlet.2005.07.083

  日期：2005.9

  New aglycon switch approach using glycosyltransferase VinC was explored to create unnatural glycosides from natural glycoside in one-pot reaction. This aglycon switch comprises from two reactions, where NDP-vicenisamine generated in situ from natural glycoside vicenistatin and NDP by the reverse reaction is transferred to the targeted additional aglycons to form unnatural vicenisaminides by the forward reaction. (c) 2005 Elsevier Ltd. All rights reserved.