2,4-Dioxo-4-[2-(trifluoromethyl)phenyl]butanoic acid | 737772-46-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2,4-Dioxo-4-[2-(trifluoromethyl)phenyl]butanoic acid
• CAS: 737772-46-2
• 化学式: C₁₁H₇F₃O₄
• 分子量: 260.169
• InChiKey: FRWVUMXUFNVNLO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.1
• 重原子数：
  18
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  71.4
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  邻三氟甲基苯乙酮 在 sodium hydroxide 、 硫酸 、 sodium hydride 作用下， 以 水 、 甲苯 为溶剂， 反应 0.5h， 生成 2,4-Dioxo-4-[2-(trifluoromethyl)phenyl]butanoic acid
  参考文献：
  名称：

  Slow-binding inhibition of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase

  摘要：

  2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase is a key enzyme in the Entner-Doudoroff pathway of bacteria. It catalyzes the reversible production of KDPG from pyruvate and D-glyceraldehyde 3-phosphate through a class I Schiff base mechanism. On the basis of aldolase mechanistic pathway, various pyruvate analogues bearing beta-diketo structures were designed and synthesized as potential inhibitors. Their capacity to inhibit aldolase catalyzed reaction by forming stabilized iminium ion or conjugated enamine were investigated by enzymatic kinetics and UV-vis difference spectroscopy. Depending of the substituent R (methyl or aromatic ring), a competitive or a slow-binding inhibition takes place. These results were examined on the basis of the three-dimensional structure of the enzyme. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2004.03.039

文献信息

• Slow-binding inhibition of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase
  作者：Rémi Braga、Laurence Hecquet、Casimir Blonski

  DOI：10.1016/j.bmc.2004.03.039

  日期：2004.6

  2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase is a key enzyme in the Entner-Doudoroff pathway of bacteria. It catalyzes the reversible production of KDPG from pyruvate and D-glyceraldehyde 3-phosphate through a class I Schiff base mechanism. On the basis of aldolase mechanistic pathway, various pyruvate analogues bearing beta-diketo structures were designed and synthesized as potential inhibitors. Their capacity to inhibit aldolase catalyzed reaction by forming stabilized iminium ion or conjugated enamine were investigated by enzymatic kinetics and UV-vis difference spectroscopy. Depending of the substituent R (methyl or aromatic ring), a competitive or a slow-binding inhibition takes place. These results were examined on the basis of the three-dimensional structure of the enzyme. (C) 2004 Elsevier Ltd. All rights reserved.