adenosine-5'-phosphoric (1-13C-hexadecanoic) anhydride

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• 英文名称: adenosine-5'-phosphoric (1-13C-hexadecanoic) anhydride
• 英文别名: [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] (113C)hexadecanoate
• 化学式: C₂₆H₄₄N₅O₈P
• 分子量: 586.627
• InChiKey: CMRDSXPYXCUXMI-AKPLUHGTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.4
• 重原子数：
  40
• 可旋转键数：
  20
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.77
• 拓扑面积：
  192
• 氢给体数：
  4
• 氢受体数：
  12

反应信息

• 作为产物：
  描述：

  1-¹³C-palmitic acid 在 lithium hydroxide 、 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 、 吡啶 、 乙醚 、 水 为溶剂， 反应 12.17h， 生成 adenosine-5'-phosphoric (1-13C-hexadecanoic) anhydride
  参考文献：
  名称：

  Characterization of Acyl Adenyl Anhydrides:  Differences in the Hydrolytic Rates of Fatty Acyl-AMP and Aminoacyl-AMP Derivatives

  摘要：

  An improved procedure has been developed to prepare RCOOPO2-Ado (R = C6H13 and C15H31), the intermediate in the enzymatic synthesis of acyl-CoA's. The product has been characterized by spectral methods which, in turn, were used to define the hydrolysis rates of RCO-AMP. When R is a fatty acyl group, the hydrolysis rate is 10-fold slower than when R is aminoacyl. In both cases, the hydrolysis rate is enhanced by Mg2+. We speculate that the rate acceleration is due to intramolecular participation of the second carbonyl group in the aminoacyl residue.

  DOI：

  10.1021/jo971874f

文献信息

• Characterization of Acyl Adenyl Anhydrides:  Differences in the Hydrolytic Rates of Fatty Acyl-AMP and Aminoacyl-AMP Derivatives
  作者：Otto F. Schall、Iwao Suzuki、Clare L. Murray、Jeffrey I. Gordon、George W. Gokel

  DOI：10.1021/jo971874f

  日期：1998.11.1

  An improved procedure has been developed to prepare RCOOPO2-Ado (R = C6H13 and C15H31), the intermediate in the enzymatic synthesis of acyl-CoA's. The product has been characterized by spectral methods which, in turn, were used to define the hydrolysis rates of RCO-AMP. When R is a fatty acyl group, the hydrolysis rate is 10-fold slower than when R is aminoacyl. In both cases, the hydrolysis rate is enhanced by Mg2+. We speculate that the rate acceleration is due to intramolecular participation of the second carbonyl group in the aminoacyl residue.