(Z)-3-ethyl-5-(4-methoxybenzylidene)-2-thioxothiazolidin-4-one | 1220624-82-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: (Z)-3-ethyl-5-(4-methoxybenzylidene)-2-thioxothiazolidin-4-one
• 英文别名: (5Z)-3-ethyl-5-[(4-methoxyphenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-4-one
• CAS: 1220624-82-7
• 化学式: C₁₃H₁₃NO₂S₂
• 分子量: 279.384
• InChiKey: LCYCDCHEFYTADW-FLIBITNWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  18
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.23
• 拓扑面积：
  86.9
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  3-乙基-2-硫代-4-噻唑烷二酮 、 4-甲氧基苯甲醛 在 sodium acetate 、 溶剂黄146 作用下， 反应 16.0h， 以53%的产率得到(Z)-3-ethyl-5-(4-methoxybenzylidene)-2-thioxothiazolidin-4-one
  参考文献：
  名称：

  Exploration of inhibitors for diaminopimelate aminotransferase

  摘要：

  Bacteria and higher plants make L-lysine from diaminopimelic acid (DAP). In mammals L-lysine is an essential amino acid that must be acquired from the diet as the biosynthetic pathway is absent for this key constituent of proteins. Recently, LL-diaminopimelate aminotransferase (LL-DAP-AT), a pyridoxal-5'-phosphate (PLP)-dependent enzyme, was reported to catalyze a key step in the route to L-lysine in plants and Chlamydia. Specific inhibitors of this enzyme could thus potentially serve as herbicides or antibiotics that are non-toxic to mammals. In this work, 29,201 inhibitors were screened against LL-DAP-AT and the IC50 values were determined for the top 46 compounds. An aryl hydrazide and rhodanine derivatives were further modified to generate 20 analogues that were also tested against LL-DAP-AT. These analogues provide additional structure-activity relationships (SAR) that are useful in guiding further design of inhibitors. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2010.02.001

文献信息

• Exploration of inhibitors for diaminopimelate aminotransferase
  作者：Chenguang Fan、Matthew D. Clay、Michael K. Deyholos、John C. Vederas

  DOI：10.1016/j.bmc.2010.02.001

  日期：2010.3

  Bacteria and higher plants make L-lysine from diaminopimelic acid (DAP). In mammals L-lysine is an essential amino acid that must be acquired from the diet as the biosynthetic pathway is absent for this key constituent of proteins. Recently, LL-diaminopimelate aminotransferase (LL-DAP-AT), a pyridoxal-5'-phosphate (PLP)-dependent enzyme, was reported to catalyze a key step in the route to L-lysine in plants and Chlamydia. Specific inhibitors of this enzyme could thus potentially serve as herbicides or antibiotics that are non-toxic to mammals. In this work, 29,201 inhibitors were screened against LL-DAP-AT and the IC50 values were determined for the top 46 compounds. An aryl hydrazide and rhodanine derivatives were further modified to generate 20 analogues that were also tested against LL-DAP-AT. These analogues provide additional structure-activity relationships (SAR) that are useful in guiding further design of inhibitors. (C) 2010 Elsevier Ltd. All rights reserved.