N⁴-(benzyl) AICAR triphosphate

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 咪唑核糖核苷和核糖核苷酸
• 英文名称: N⁴-(benzyl) AICAR triphosphate
• 英文别名: [[(2R,3S,4R,5R)-5-[5-amino-4-(benzylcarbamoyl)imidazol-1-yl]-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate
• 化学式: C₁₆H₂₃N₄O₁₄P₃
• 分子量: 588.298
• InChiKey: UEVOJYDJRJHITP-XNIJJKJLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.1
• 重原子数：
  37
• 可旋转键数：
  11
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  282
• 氢给体数：
  8
• 氢受体数：
  16

反应信息

• 作为产物：
  描述：

  5-amino-1-(β-D-ribofuranosyl)imidazole-4-(N-benzyl)carboxamide 在 磷酸三甲酯 、 三丁基焦磷酸铵 、 三氯氧磷 作用下， 生成 N⁴-(benzyl) AICAR triphosphate
  参考文献：
  名称：

  Conformational restraint is a critical determinant of unnatural nucleotide recognition by protein kinases

  摘要：

  This report describes the synthesis of N-4-(benzyl) AICAR triphosphate, a conformationally restrained analogue of N-4-(benzyl) ribavirin triphosphate. Both of these nucleotides were evaluated as phosphodonors for wild-type p38 MAP kinase and T106G p38MAP kinase, a designed mutant with expanded nucleotide specificity. The conformationally restrained nucleotide, N-4-(benzyl) AICAR triphosphate, is orthogonal to (not accepted as a substrate by) wild-type p38MAP kinase, in contrast to N-4-(benzyl) ribavirin triphosphate. Furthermore, N-4-(benzyl) AICAR triphosphate, is accepted as a substrate by T106G p38 MAP kinase, in contrast to N-4-(benzyl) ribavirin triphosphate. We hypothesize that the presence of an internal hydrogen bond in N-4-(benzyl) AICAR and its absence in N-4-(benzyl) ribavirin triphosphate is the main determinant for their differing structure-activity relationships. (C) 2002 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(02)00616-9

文献信息

• Conformational restraint is a critical determinant of unnatural nucleotide recognition by protein kinases
  作者：Scott M Ulrich、Nathan A Sallee、Kevan M Shokat

  DOI：10.1016/s0960-894x(02)00616-9

  日期：2002.11

  This report describes the synthesis of N-4-(benzyl) AICAR triphosphate, a conformationally restrained analogue of N-4-(benzyl) ribavirin triphosphate. Both of these nucleotides were evaluated as phosphodonors for wild-type p38 MAP kinase and T106G p38MAP kinase, a designed mutant with expanded nucleotide specificity. The conformationally restrained nucleotide, N-4-(benzyl) AICAR triphosphate, is orthogonal to (not accepted as a substrate by) wild-type p38MAP kinase, in contrast to N-4-(benzyl) ribavirin triphosphate. Furthermore, N-4-(benzyl) AICAR triphosphate, is accepted as a substrate by T106G p38 MAP kinase, in contrast to N-4-(benzyl) ribavirin triphosphate. We hypothesize that the presence of an internal hydrogen bond in N-4-(benzyl) AICAR and its absence in N-4-(benzyl) ribavirin triphosphate is the main determinant for their differing structure-activity relationships. (C) 2002 Elsevier Science Ltd. All rights reserved.