2-chloro-6-nitro-α-bromoacetophenone | 175657-82-6

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-chloro-6-nitro-α-bromoacetophenone
• 英文别名: 2-Bromo-1-(2-chloro-6-nitrophenyl)ethanone
• CAS: 175657-82-6
• 化学式: C₈H₅BrClNO₃
• 分子量: 278.49
• InChiKey: UCNKBWCIRRWOIA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  14
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  62.9
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  2-chloro-6-nitro-α-bromoacetophenone 在 盐酸 、 potassium tert-butylate 、 铁粉 、 溶剂黄146 作用下， 反应 26.0h， 生成 6-chlorokynurenine dihydrochloride
  参考文献：
  名称：

  Derivatives of kynurenine as inhibitors of rat brain kynurenine aminotransferase

  摘要：

  The structural requirements of the catalytic site of kynurenine aminotransferase (KAT), the enzyme responsible for the conversion of L-kynurenine (KYN) to kynurenic acid (KYNA), were examined using analogs and derivatives of KYN: KYNA production from KYN was monitored in rat brain homogenates and brain tissue slices. Modification of KYN's acylalanine side chain or its ring amino group resulted in compounds which did not substantially affect KYNA synthesis. Ring chlorination in positions 3, 4, 5 and 6 yielded KYN analogs which interfered with KYNA production. L-5-Cl-KYN was the most active of the chlorinated kynurenines, and one of the most potent of several other 5-substituted kynurenines. L-5-Cl-KYN was an excellent substrate of KAT, yielding 6-Cl-KYNA. Finally, in kinetic studies, L-5-Cl-KYN (K-i = 5.4 mu M) was found to have an approximately five times higher affinity to the enzyme than the natural substrate KYN (K-m = 28 mu M).

  DOI：

  10.1016/s0223-5234(96)80002-x
• 作为产物：
  描述：

  2'-氯-6'-硝基苯乙酮 在 溴 作用下， 以 乙醚 为溶剂， 反应 2.0h， 生成 2-chloro-6-nitro-α-bromoacetophenone
  参考文献：
  名称：

  Derivatives of kynurenine as inhibitors of rat brain kynurenine aminotransferase

  摘要：

  The structural requirements of the catalytic site of kynurenine aminotransferase (KAT), the enzyme responsible for the conversion of L-kynurenine (KYN) to kynurenic acid (KYNA), were examined using analogs and derivatives of KYN: KYNA production from KYN was monitored in rat brain homogenates and brain tissue slices. Modification of KYN's acylalanine side chain or its ring amino group resulted in compounds which did not substantially affect KYNA synthesis. Ring chlorination in positions 3, 4, 5 and 6 yielded KYN analogs which interfered with KYNA production. L-5-Cl-KYN was the most active of the chlorinated kynurenines, and one of the most potent of several other 5-substituted kynurenines. L-5-Cl-KYN was an excellent substrate of KAT, yielding 6-Cl-KYNA. Finally, in kinetic studies, L-5-Cl-KYN (K-i = 5.4 mu M) was found to have an approximately five times higher affinity to the enzyme than the natural substrate KYN (K-m = 28 mu M).

  DOI：

  10.1016/s0223-5234(96)80002-x

文献信息

• Derivatives of kynurenine as inhibitors of rat brain kynurenine aminotransferase
  作者：M Varasi、A Della Torre、F Heidempergher、P Pevarello、C Speciale、P Guidetti、DR Wells、R Schwarcz

  DOI：10.1016/s0223-5234(96)80002-x

  日期：1996.1

  The structural requirements of the catalytic site of kynurenine aminotransferase (KAT), the enzyme responsible for the conversion of L-kynurenine (KYN) to kynurenic acid (KYNA), were examined using analogs and derivatives of KYN: KYNA production from KYN was monitored in rat brain homogenates and brain tissue slices. Modification of KYN's acylalanine side chain or its ring amino group resulted in compounds which did not substantially affect KYNA synthesis. Ring chlorination in positions 3, 4, 5 and 6 yielded KYN analogs which interfered with KYNA production. L-5-Cl-KYN was the most active of the chlorinated kynurenines, and one of the most potent of several other 5-substituted kynurenines. L-5-Cl-KYN was an excellent substrate of KAT, yielding 6-Cl-KYNA. Finally, in kinetic studies, L-5-Cl-KYN (K-i = 5.4 mu M) was found to have an approximately five times higher affinity to the enzyme than the natural substrate KYN (K-m = 28 mu M).