(Z)-N-(5-benzylidene-4-oxo-2-thioxothiazolidin-3-yl)acetamide | 1220624-94-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 唑烷类
• 英文名称: (Z)-N-(5-benzylidene-4-oxo-2-thioxothiazolidin-3-yl)acetamide
• 英文别名: N-[(5Z)-5-benzylidene-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]acetamide
• CAS: 1220624-94-1
• 化学式: C₁₂H₁₀N₂O₂S₂
• 分子量: 278.356
• InChiKey: RWDWDRUNVYTQNT-YFHOEESVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  18
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.08
• 拓扑面积：
  107
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  N-(4-氧代-2-硫氧代-噻唑啉-3-基)-乙酰胺 、 苯甲醛 在 sodium acetate 、 溶剂黄146 作用下， 反应 16.0h， 以88%的产率得到(Z)-N-(5-benzylidene-4-oxo-2-thioxothiazolidin-3-yl)acetamide
  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.