2-Allyloxy-benzo[d][1,3]oxazin-4-one | 184944-83-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并恶嗪类
• 英文名称: 2-Allyloxy-benzo[d][1,3]oxazin-4-one
• 英文别名: 2-Prop-2-enoxy-3,1-benzoxazin-4-one
• CAS: 184944-83-0
• 化学式: C₁₁H₉NO₃
• 分子量: 203.197
• InChiKey: YXDVRUYLFGEDSW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  15
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.09
• 拓扑面积：
  47.9
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  邻氨基苯甲酸 、 氯甲酸烯丙酯 以 吡啶 为溶剂， 生成 2-Allyloxy-benzo[d][1,3]oxazin-4-one
  参考文献：
  名称：

  Inhibition of HSV-1 protease by benzoxazinones

  摘要：

  Benzoxazinones have been discovered which are mechanism based inhibitors of HSV-1 protease with micromolar IC50 values. Formation of a monoadduct consistent with the acyl-enzyme complex was detected by mass spectroscopy. A parallel array synthesis was developed to explore 2-heteroatom substituted SAR. Copyright (C) 1996 Elsevier Science Ltd

  DOI：

  10.1016/0960-894x(96)00455-6

文献信息

• Inhibition of HSV-1 protease by benzoxazinones
  作者：Richard L. Jarvest、Martin J. Parratt、Christine M. Debouck、Joselina G. Gorniak、L. John Jennings、Halina T. Serafinowska、James E. Strickler

  DOI：10.1016/0960-894x(96)00455-6

  日期：1996.10

  Benzoxazinones have been discovered which are mechanism based inhibitors of HSV-1 protease with micromolar IC50 values. Formation of a monoadduct consistent with the acyl-enzyme complex was detected by mass spectroscopy. A parallel array synthesis was developed to explore 2-heteroatom substituted SAR. Copyright (C) 1996 Elsevier Science Ltd
• Inhibition of cathepsin G by 4H-3,1-benzoxazin-4-ones
  作者：Michael Gütschow、Ulf Neumann

  DOI：10.1016/s0968-0896(97)00128-4

  日期：1997.10

  A series of 4H-3,1-benzoxazin-4-ones is reported that inhibit the serine proteases human cathepsin G and bovine chymotrypsin. The synthesis and kinetic parameters of the alkaline hydrolysis is described. These compounds act as acyl-enzyme inhibitors of both enzymes. The reaction of cathepsin G with 2-benzylamino-4H-3,1-benzoxazin-4-one (20) was studied in detail. A partition in deacylation of the initially formed acyl-enzyme was observed, leading to the formation of 2-(3-benzylureido)benzoic acid (26) and 3-benzylquinazoline-2,4-(1H,3H)-dione (27). A 6-methyl substitution strongly increased the acylation rate of both proteases. Introduction of an aryl moiety into the 2-substituent led to compounds with K-i values towards cathepsin G in the nanomolar range. Their inhibitory potency is stronger than that of other synthetic inhibitors of cathepsin G. (C) 1997 Elsevier Science Ltd.