6-Amino-5-bromopyrimidin-4(3H)-one | 6312-71-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: 6-Amino-5-bromopyrimidin-4(3H)-one
• 英文别名: 4-amino-5-bromo-1H-pyrimidin-6-one
• CAS: 6312-71-6
• 化学式: C₄H₄BrN₃O
• 分子量: 189.999
• InChiKey: HZDFWPAVCWGZPV-UHFFFAOYSA-N

物化性质

• 熔点：
  268℃ (water )
• 沸点：
  220.4±50.0 °C(Predicted)
• 密度：
  2.25±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  9
• 可旋转键数：
  0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  67.5
• 氢给体数：
  2
• 氢受体数：
  3

安全信息

• 海关编码：
  2933599090

反应信息

• 作为反应物：
  描述：

  6-Amino-5-bromopyrimidin-4(3H)-one 在 bovine buttermilk xanthine oxidase 作用下， 以 phosphate buffer 为溶剂， 生成 5-溴-6-氨基尿嘧啶
  参考文献：
  名称：

  Xanthine oxidase-activated prodrugs of thymidine phosphorylase inhibitors

  摘要：

  Thymidine phosphorylase (TP) is over-expressed in various tumour types and plays an important role in tumour angiogenesis, growth, invasion and metastasis. The enzymatic activity of TP is required for the angiogenic effect of TP, therefore, inhibitors of TP are of significant interest in cancer chemotherapy. A series of xanthine oxidase (XO) activated prodrugs of known inhibitors of TP have been designed and synthesized with the ultimate intent of improving tumour selectivity and pharmacokinetic characteristics. These prodrugs were not inhibitors of TP, but were selectively oxidized by XO at C-2 and/or C-4 of the uracil ring moiety to generate the desired TP inhibitor. Molecular modelling of both the TP inhibitors and XO-activated prodrugs rationalized their binding in the active site of the human TP crystal structure. (c) 2007 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2007.07.015
• 作为产物：
  描述：

  4-氨基-6-羟基嘧啶 在 溴 作用下， 以 水 为溶剂， 反应 1.0h， 以47.3%的产率得到6-Amino-5-bromopyrimidin-4(3H)-one
  参考文献：
  名称：

  Xanthine oxidase-activated prodrugs of thymidine phosphorylase inhibitors

  摘要：

  Thymidine phosphorylase (TP) is over-expressed in various tumour types and plays an important role in tumour angiogenesis, growth, invasion and metastasis. The enzymatic activity of TP is required for the angiogenic effect of TP, therefore, inhibitors of TP are of significant interest in cancer chemotherapy. A series of xanthine oxidase (XO) activated prodrugs of known inhibitors of TP have been designed and synthesized with the ultimate intent of improving tumour selectivity and pharmacokinetic characteristics. These prodrugs were not inhibitors of TP, but were selectively oxidized by XO at C-2 and/or C-4 of the uracil ring moiety to generate the desired TP inhibitor. Molecular modelling of both the TP inhibitors and XO-activated prodrugs rationalized their binding in the active site of the human TP crystal structure. (c) 2007 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2007.07.015

文献信息

• Synthesis and enzymatic evaluation of xanthine oxidase-activated prodrugs based on inhibitors of thymidine phosphorylase
  作者：Philip Reigan、Abdul Gbaj、Edwin Chinje、Ian J. Stratford、Kenneth T. Douglas、Sally Freeman

  DOI：10.1016/j.bmcl.2004.08.036

  日期：2004.11

  A series of xanthine oxidase-activated prodrugs of known inhibitors of thymidine phosphorylase has been designed and synthesised to introduce turnout selectivity. These prodrugs were oxidised by xanthine oxidase at C-2 and/or C-4 of the uracil ring to generate the desired TP inhibitor. (C) 2004 Elsevier Ltd. All rights reserved.
• Xanthine oxidase-activated prodrugs of thymidine phosphorylase inhibitors
  作者：Philip Reigan、Abdul Gbaj、Ian J. Stratford、Richard A. Bryce、Sally Freeman

  DOI：10.1016/j.ejmech.2007.07.015

  日期：2008.6

  Thymidine phosphorylase (TP) is over-expressed in various tumour types and plays an important role in tumour angiogenesis, growth, invasion and metastasis. The enzymatic activity of TP is required for the angiogenic effect of TP, therefore, inhibitors of TP are of significant interest in cancer chemotherapy. A series of xanthine oxidase (XO) activated prodrugs of known inhibitors of TP have been designed and synthesized with the ultimate intent of improving tumour selectivity and pharmacokinetic characteristics. These prodrugs were not inhibitors of TP, but were selectively oxidized by XO at C-2 and/or C-4 of the uracil ring moiety to generate the desired TP inhibitor. Molecular modelling of both the TP inhibitors and XO-activated prodrugs rationalized their binding in the active site of the human TP crystal structure. (c) 2007 Elsevier Masson SAS. All rights reserved.