2-(3-diethylthioureido)benzonitrile

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2-(3-diethylthioureido)benzonitrile
• 英文别名: 3-(2-Cyanophenyl)-1,1-diethylthiourea
• 化学式: C₁₂H₁₅N₃S
• 分子量: 233.337
• InChiKey: GZGGKOQGNMSWJI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  71.2
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  2-(3-diethylthioureido)benzonitrile 在 盐酸 、 碳酸氢钠 作用下， 生成 2-diethylamino-4H-3,1-benzothiazin-4-one
  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
• 作为产物：
  描述：

  2-氨基苯甲腈 以 二氯甲烷 、 水 、 乙腈 为溶剂， 反应 4.0h， 生成 2-(3-diethylthioureido)benzonitrile
  参考文献：
  名称：

  硫代亚氨酸盐的原位生成和捕获：对4-acylimino-4 H -3,1-苯并噻嗪的分子间串联反应†

  摘要：

  2- thioureidobenzonitriles至4-酰亚氨基-4-质子催化转化ħ -3,1-苯并噻嗪是通过用羧酸酐，酰氯或氯甲酸烷基酯来完成的。该反应涉及环化成4-亚氨基-3，1-苯并噻嗪鎓盐，其硫代亚氨酸酯结构被随后与酰基供体的反应所俘获。2-脲基苄腈不进行这样的分子间串联反应。两种类型底物的不同反应行为均通过NMR监测并使用18 O富集水进行了验证。

  DOI：

  10.1039/c6ra00196c

文献信息

• PAZDERA, PAVEL;ONDRACEK, DRAHOSLAV
  作者：PAZDERA, PAVEL、ONDRACEK, DRAHOSLAV

  DOI：——

  日期：——
• In situ generation and trapping of thioimidates: an intermolecular tandem reaction to 4-acylimino-4H-3,1-benzothiazines
  作者：Christian Steinebach、Anna-Christina Schulz-Fincke、Gregor Schnakenburg、Michael Gütschow

  DOI：10.1039/c6ra00196c

  日期：——

  accomplished by treatment with carboxylic anhydrides, acid chlorides or alkyl chloroformates. The reaction involves a cyclization to 4-imino-3,1-benzothiazinium salts, whose thioimidate structure is trapped by a subsequent reaction with the acyl donor. 2-Ureidobenzonitriles do not undergo such an intermolecular tandem reaction. The different reaction behavior of both types of substrates was verified by

  2- thioureidobenzonitriles至4-酰亚氨基-4-质子催化转化ħ -3,1-苯并噻嗪是通过用羧酸酐，酰氯或氯甲酸烷基酯来完成的。该反应涉及环化成4-亚氨基-3，1-苯并噻嗪鎓盐，其硫代亚氨酸酯结构被随后与酰基供体的反应所俘获。2-脲基苄腈不进行这样的分子间串联反应。两种类型底物的不同反应行为均通过NMR监测并使用18 O富集水进行了验证。
• 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.