4-amino-1-[(2R,5S)-5-[(4-oxo-1,3,2-benzodioxaphosphinin-2-yl)oxymethyl]oxolan-2-yl]pyrimidin-2-one | 688804-54-8

• 分子结构分类: 有机化合物 - 苯类化合物
• 英文名称: 4-amino-1-[(2R,5S)-5-[(4-oxo-1,3,2-benzodioxaphosphinin-2-yl)oxymethyl]oxolan-2-yl]pyrimidin-2-one
• CAS: 688804-54-8
• 化学式: C₁₆H₁₆N₃O₆P
• 分子量: 377.293
• InChiKey: ZDAOKRCPOLNCQU-NSQKUDKHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.0
• 重原子数：
  26.0
• 可旋转键数：
  4.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  114.9
• 氢给体数：
  1.0
• 氢受体数：
  9.0

反应信息

• 作为反应物：
  描述：

  4-amino-1-[(2R,5S)-5-[(4-oxo-1,3,2-benzodioxaphosphinin-2-yl)oxymethyl]oxolan-2-yl]pyrimidin-2-one 在 borane-N,N-diisopropylethylamine complex 、 水 、 三丁基焦磷酸铵 、 三乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 17.0h， 生成 N³-borano-2',3'-dideoxycytidine 5'-(α-P-borano)triphosphate
  参考文献：
  名称：

  Incorporation of (α-P-Borano)-2′,3′-dideoxycytidine 5′-Triphosphate into DNA by Drug-Resistant MMLV Reverse Transcriptase andTaqDNA Polymerase

  摘要：

  The Rp-stereoisomer of 5'-(alpha-P-borano)triphosphates of 2'-deoxycytidine (Rp-dCTPalphaB) and 2',3'-dideoxycytidine (Rp-ddCTPalphaB) were synthesized. Their steady-state kinetics of incorporation by ddNTP-resistant enzymes, e.g., MMLV reverse transcriptase (RT) and Taq DNA polymerase, were investigated and compared with incorporation of dCTP and ddCTP. The alpha-boranophosphate substitution in ddCTP results in a 28-fold increase in efficiency of incorporation of theRp-ddCTPalphaB isomer by MMLV RT, yet has minimal effect on the efficiency of incorporation by Taq DNA polymerase.

  DOI：

  10.1081/ncn-120023091
• 作为产物：
  描述：

  2-氯-1,3,2-苯并二氧磷杂环己烷-4-酮 、 2,3-二脱氧胞啶 在 吡啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.25h， 生成 4-amino-1-[(2R,5S)-5-[(4-oxo-1,3,2-benzodioxaphosphinin-2-yl)oxymethyl]oxolan-2-yl]pyrimidin-2-one
  参考文献：
  名称：

  Incorporation of (α-P-Borano)-2′,3′-dideoxycytidine 5′-Triphosphate into DNA by Drug-Resistant MMLV Reverse Transcriptase andTaqDNA Polymerase

  摘要：

  The Rp-stereoisomer of 5'-(alpha-P-borano)triphosphates of 2'-deoxycytidine (Rp-dCTPalphaB) and 2',3'-dideoxycytidine (Rp-ddCTPalphaB) were synthesized. Their steady-state kinetics of incorporation by ddNTP-resistant enzymes, e.g., MMLV reverse transcriptase (RT) and Taq DNA polymerase, were investigated and compared with incorporation of dCTP and ddCTP. The alpha-boranophosphate substitution in ddCTP results in a 28-fold increase in efficiency of incorporation of theRp-ddCTPalphaB isomer by MMLV RT, yet has minimal effect on the efficiency of incorporation by Taq DNA polymerase.

  DOI：

  10.1081/ncn-120023091