Dimethyl 5-[(4-nitrophenyl)carbamoyl]benzene-1,3-dicarboxylate | 1374006-64-0

• 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: Dimethyl 5-[(4-nitrophenyl)carbamoyl]benzene-1,3-dicarboxylate
• CAS: 1374006-64-0
• 化学式: C₁₇H₁₄N₂O₇
• 分子量: 358.307
• InChiKey: JBFPVVBYJNOLOX-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  26
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  128
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  甲醇 、 5-(4-Nitrophenylcarbamoyl)Isophthalic Acid 在 硫酸 作用下， 以70%的产率得到Dimethyl 5-[(4-nitrophenyl)carbamoyl]benzene-1,3-dicarboxylate
  参考文献：
  名称：

  Molecular docking and enzymatic evaluation to identify selective inhibitors of aspartate semialdehyde dehydrogenase

  摘要：

  Microbes that have gained resistance against antibiotics pose a major emerging threat to human health. New targets must be identified that will guide the development of new classes of antibiotics. The selective inhibition of key microbial enzymes that are responsible for the biosynthesis of essential metabolites can be an effective way to counter this growing threat. Aspartate semialdehyde dehydrogenases (ASADHs) produce an early branch point metabolite in a microbial biosynthetic pathway for essential amino acids and for quorum sensing molecules. In this study, molecular modeling and docking studies were performed to achieve two key objectives that are important for the identification of new selective inhibitors of ASADH. First, virtual screening of a small library of compounds was used to identify new core structures that could serve as potential inhibitors of the ASADHs. Compounds have been identified from diverse chemical classes that are predicted to bind to ASADH with high affinity. Next, molecular docking studies were used to prioritize analogs within each class for synthesis and testing against representative bacterial forms of ASADH from Streptococcus pneumoniae and Vibrio cholerae. These studies have led to new micromolar inhibitors of ASADH, demonstrating the utility of this molecular modeling and docking approach for the identification of new classes of potential enzyme inhibitors. (C) 2012 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2012.03.013

文献信息

• Molecular docking and enzymatic evaluation to identify selective inhibitors of aspartate semialdehyde dehydrogenase
  作者：Amarjit Luniwal、Lin Wang、Alexander Pavlovsky、Paul W. Erhardt、Ronald E. Viola

  DOI：10.1016/j.bmc.2012.03.013

  日期：2012.5

  Microbes that have gained resistance against antibiotics pose a major emerging threat to human health. New targets must be identified that will guide the development of new classes of antibiotics. The selective inhibition of key microbial enzymes that are responsible for the biosynthesis of essential metabolites can be an effective way to counter this growing threat. Aspartate semialdehyde dehydrogenases (ASADHs) produce an early branch point metabolite in a microbial biosynthetic pathway for essential amino acids and for quorum sensing molecules. In this study, molecular modeling and docking studies were performed to achieve two key objectives that are important for the identification of new selective inhibitors of ASADH. First, virtual screening of a small library of compounds was used to identify new core structures that could serve as potential inhibitors of the ASADHs. Compounds have been identified from diverse chemical classes that are predicted to bind to ASADH with high affinity. Next, molecular docking studies were used to prioritize analogs within each class for synthesis and testing against representative bacterial forms of ASADH from Streptococcus pneumoniae and Vibrio cholerae. These studies have led to new micromolar inhibitors of ASADH, demonstrating the utility of this molecular modeling and docking approach for the identification of new classes of potential enzyme inhibitors. (C) 2012 Elsevier Ltd. All rights reserved.