2-amino-3H,5H-7-(4-iodobenzoyl)pyrrolo[3,2-d]pyrimidin-4-one

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-amino-3H,5H-7-(4-iodobenzoyl)pyrrolo[3,2-d]pyrimidin-4-one
• 英文别名: 2-Amino-7-(4-iodobenzoyl)-3,5-dihydropyrrolo[3,2-d]pyrimidin-4-one；2-amino-7-(4-iodobenzoyl)-3,5-dihydropyrrolo[3,2-d]pyrimidin-4-one
• 化学式: C₁₃H₉IN₄O₂
• 分子量: 380.145
• InChiKey: APHXZZHIZPWWHM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.2
• 重原子数：
  20
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  100
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  2-氨基-6-甲基-5-硝基-3H-嘧啶-4-酮 在 sodium dithionite 、 三氟甲磺酸 作用下， 以 水 为溶剂， 反应 76.0h， 生成 2-amino-3H,5H-7-(4-iodobenzoyl)pyrrolo[3,2-d]pyrimidin-4-one
  参考文献：
  名称：

  9-Benzoyl 9-deazaguanines as potent xanthine oxidase inhibitors

  摘要：

  A novel potent xanthine oxidase inhibitor, 3-nitrobenzoyl 9-deazaguanine (LSPN451), was selected from a series of 10 synthetic derivatives. The enzymatic assays were carried out using an on-flow bidimensional liquid chromatography (2D LC) system, which allowed the screening, the measurement of the kinetic inhibition constant and the characterization of the inhibition mode. This compound showed a non-competitive inhibition mechanism with more affinity for the enzyme-substrate complex than for the free enzyme, and inhibition constant of 55.1 +/- 9.80 nM, about thirty times more potent than allopurinol. Further details of synthesis and enzymatic studies are presented herein. (c) 2015 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2015.12.006

文献信息

• 9-Benzoyl 9-deazaguanines as potent xanthine oxidase inhibitors
  作者：Marili V.N. Rodrigues、Alexandre F. Barbosa、Júlia F. da Silva、Deborah A. dos Santos、Kenia L. Vanzolini、Marcela C. de Moraes、Arlene G. Corrêa、Quezia B. Cass

  DOI：10.1016/j.bmc.2015.12.006

  日期：2016.1

  A novel potent xanthine oxidase inhibitor, 3-nitrobenzoyl 9-deazaguanine (LSPN451), was selected from a series of 10 synthetic derivatives. The enzymatic assays were carried out using an on-flow bidimensional liquid chromatography (2D LC) system, which allowed the screening, the measurement of the kinetic inhibition constant and the characterization of the inhibition mode. This compound showed a non-competitive inhibition mechanism with more affinity for the enzyme-substrate complex than for the free enzyme, and inhibition constant of 55.1 +/- 9.80 nM, about thirty times more potent than allopurinol. Further details of synthesis and enzymatic studies are presented herein. (c) 2015 Elsevier Ltd. All rights reserved.