2-(3-苯甲酰脲基)苯甲酸 | 163683-00-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 中文名称: 2-(3-苯甲酰脲基)苯甲酸
• 英文名称: 2-(3-benzoylureido)benzoic acid
• 英文别名: N-benzoylcarbamoyl-anthranilic acid；N-Benzoylcarbamoyl-anthranilsaeure；2-(ω-Benzoyl-ureido)-benzoesaeure；N-(2-Carboxy-phenyl)-N'-benzoyl-harnstoff；2-{[(Benzoylamino)carbonyl]amino}benzoic acid；2-(benzoylcarbamoylamino)benzoic acid
• CAS: 163683-00-9
• 化学式: C₁₅H₁₂N₂O₄
• 分子量: 284.271
• InChiKey: SYPMVRRIFVLKFE-UHFFFAOYSA-N

物化性质

• 密度：
  1.398±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  21
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  95.5
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-(3-苯甲酰脲基)苯甲酸 生成 苯甲酸 、 alkaline earth salt of/the/ methylsulfuric acid
  参考文献：
  名称：

  Scott; Cohen, Journal of the Chemical Society, 1921, vol. 119, p. 665

  摘要：

  DOI：
• 作为产物：
  描述：

  2-Benzoylamino-4h-3,1-benzoxazin-4-one 在 3-(cyclohexylamino)propanesulfonic acid buffer 、 水 作用下， 以 乙腈 为溶剂， 生成 2-(3-苯甲酰脲基)苯甲酸
  参考文献：
  名称：

  3,1-Benzothiazin-4-ones and 3,1-Benzoxazin-4-ones: Highly Different Activities in Chymotrypsin Inactivation

  摘要：

  3,1-Benzothiazin-4-ones are suIfur analogs of the potent serine protease inactivators of the 3, l-benzoxazin-4-one type, which acylate the serine residue within the active site of the enzymes. A series of 2-amino-3,1-benzothiazinones was synthesized, but these compounds showed only very little inhibitory activity toward chymotrypsin, a model serine protease. Detailed investigations revealed that benzothiazinones and benzoxazinones react with identical mechanisms, but benzothiazinones acylate chymotrypsin with much lower rate constants. Investigations of nonenzymatic hydrolysis showed the benzothiazinones to be intrinsically more stable than benzoxazinones. It was concluded from spectroscopic results, that benzoxazinones are highly activated due to the absence of ester-like resonance. 2-Benzoylamino-4H-3,1-benzoxazin-4-one was found to be a new, highly active chymotrypsin inactivator. In contrast, benzothiazinones were found to be resonance stabilized. The contribution of a resonance structure with an exocyclic oxanion to the overall structure of the benzothiazinones and its nonproductive binding to the active site explained their low reactivity toward chymotrypsin. (C) 1995 Academic Press, Inc.

  DOI：

  10.1006/bioo.1995.1006

文献信息

• 2-Benzoylamino-6,7-dimethoxy-4H-3,1-benzoxazin-4-one: Synthesis and investigation of serine protease inactivation
  作者：M. G�tschow、U. Neumann

  DOI：10.1007/bf00811383

  日期：1995.10

  2-Benzoylamino-6,7-dimethoxy-4H-3,1-benzoxazin-4-one was prepared by thermal treatment of 2-(3-benzoylthioureido)-4,5-dimethoxybenzoic acid and by benzoylation of 2-amino-6,7-dimethoxy-4H-3,1-benzoxazin-4-one. The inactivation of chymotrypsin and human leukozyte elastase by the title compound and 2-benzoylamino-4H-3,1-benzoxazin-4-one is reported.
• Scott; Cohen, Journal of the Chemical Society, 1921, vol. 119, p. 665
  作者：Scott、Cohen

  DOI：——

  日期：——
• 3,1-Benzothiazin-4-ones and 3,1-Benzoxazin-4-ones: Highly Different Activities in Chymotrypsin Inactivation
  作者：U. Neumann、M. Gutschow

  DOI：10.1006/bioo.1995.1006

  日期：1995.3

  3,1-Benzothiazin-4-ones are suIfur analogs of the potent serine protease inactivators of the 3, l-benzoxazin-4-one type, which acylate the serine residue within the active site of the enzymes. A series of 2-amino-3,1-benzothiazinones was synthesized, but these compounds showed only very little inhibitory activity toward chymotrypsin, a model serine protease. Detailed investigations revealed that benzothiazinones and benzoxazinones react with identical mechanisms, but benzothiazinones acylate chymotrypsin with much lower rate constants. Investigations of nonenzymatic hydrolysis showed the benzothiazinones to be intrinsically more stable than benzoxazinones. It was concluded from spectroscopic results, that benzoxazinones are highly activated due to the absence of ester-like resonance. 2-Benzoylamino-4H-3,1-benzoxazin-4-one was found to be a new, highly active chymotrypsin inactivator. In contrast, benzothiazinones were found to be resonance stabilized. The contribution of a resonance structure with an exocyclic oxanion to the overall structure of the benzothiazinones and its nonproductive binding to the active site explained their low reactivity toward chymotrypsin. (C) 1995 Academic Press, Inc.