2-Amino-4-azido-6-methoxy-1,3,5-triazin | 5248-73-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 三嗪类
• 英文名称: 2-Amino-4-azido-6-methoxy-1,3,5-triazin
• 英文别名: 4-azido-6-methoxy-[1,3,5]triazin-2-ylamine；4-Azido-6-methoxy-1,3,5-triazin-2-amine
• CAS: 5248-73-7
• 化学式: C₄H₅N₇O
• 分子量: 167.13
• InChiKey: UVYKKURCSDLWKK-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.2
• 重原子数：
  12
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  88.3
• 氢给体数：
  1
• 氢受体数：
  7

安全信息

• 海关编码：
  2933699090

反应信息

• 作为反应物：
  描述：

  2-Amino-4-azido-6-methoxy-1,3,5-triazin 在 一水合肼 作用下， 以 乙醇 为溶剂， 生成 N-(3-methoxy-1H-1,2,4-triazol-5-yl)-2H-tetrazol-5-amine
  参考文献：
  名称：

  Azev, Yu. A.; Gusel'nikova, O. L.; Klyuev, N. A., Russian Journal of Organic Chemistry, 1995, vol. 31, # 10, p. 1418 - 1424

  摘要：

  DOI：
• 作为产物：
  描述：

  4-氯-6-甲氧基-1,3,5-三嗪-2-胺 在 sodium azide 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 3.0h， 以72%的产率得到2-Amino-4-azido-6-methoxy-1,3,5-triazin
  参考文献：
  名称：

  Inhibition of Acetolactate Synthase Isozyme II fromEscherichia coliby a New Azido-Photoaffinity Sulfonylurea

  摘要：

  The sulfonylurea herbicides are very potent inhibitors of acetolactate synthase (ALS). These compounds have been reported as "extraneous inhibitors" due to the fact that their inhibition site corresponds to neither the catalytic site nor the regulatory sites of the enzyme. So far, the complexity of the ALS reaction and the reversible binding mode of sulfonylureas have hampered any attempt to locate the inhibitor domain. Toward this goal, a photoactivatable azidosulfonylurea has been synthesized. The azido derivative was analyzed for its photochemical and in vitro biological properties toward the bacterial ALS isozyme II. Similar to other ALS inhibitors, azidosulfonylurea potently inhibited ALS II with estimated initial and final dissociation K(i) constant values of 52 and 300 nM, respectively, and slowly inactivated the enzyme. After inhibition, removal of the free azido inhibitor and precipitation with ammonium sulfate of the azidosulfonylurea/ALS II complex led to complete though slow recovery of the enzyme activity. Following photoreaction of the inhibited complex and removal of the free inhibitor under the same conditions, the bacterial enzyme conversely exhibited stable inactivation. These results suggest that the newly synthesized azidosulfonylurea is capable of undergoing covalent reaction with ALS II, and hence it might be useful, once radiolabeled, to shed light on the inhibitor binding site of ALS. (C) 1997 Academic Press.

  DOI：

  10.1006/bioo.1997.1071