N-[5-[(4-methoxyphenyl)methyl]-1,3,4-thiadiazol-2-yl]naphthalene-1-sulfonamide | 1392281-36-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: N-[5-[(4-methoxyphenyl)methyl]-1,3,4-thiadiazol-2-yl]naphthalene-1-sulfonamide
• CAS: 1392281-36-5
• 化学式: C₂₀H₁₇N₃O₃S₂
• 分子量: 411.505
• InChiKey: YWJXGXSRIUYJMH-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.4
• 重原子数：
  28
• 可旋转键数：
  6
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  118
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  对甲氧基苯乙酸 在 吡啶 、 三氯氧磷 作用下， 反应 4.75h， 生成 N-[5-[(4-methoxyphenyl)methyl]-1,3,4-thiadiazol-2-yl]naphthalene-1-sulfonamide
  参考文献：
  名称：

  Divergent effects of compounds on the hydrolysis and transpeptidation reactions of γ-glutamyl transpeptidase

  摘要：

  A novel class of inhibitors of the enzyme gamma-glutamyl transpeptidase (GGT) were evaluated. The analog OU749 was shown previously to be an uncompetitive inhibitor of the GGT transpeptidation reaction. The data in this study show that it is an equally potent uncompetitive inhibitor of the hydrolysis reaction, the primary reaction catalyzed by GGT in vivo. A series of structural analogs of OU749 were evaluated. For many of the analogs, the potency of the inhibition differed between the hydrolysis and transpeptidation reactions, providing insight into the malleability of the active site of the enzyme. Analogs with electron withdrawing groups on the benzosulfonamide ring, accelerated the hydrolysis reaction, but inhibited the transpeptidation reaction by competing with a dipeptide acceptor. Several of the OU749 analogs inhibited the transpeptidation reaction by slow onset kinetics, similar to acivicin. Further development of inhibitors of the GGT hydrolysis reaction is necessary to provide new therapeutic compounds.

  DOI：

  10.3109/14756366.2011.597748

文献信息

• Divergent effects of compounds on the hydrolysis and transpeptidation reactions of γ-glutamyl transpeptidase
  作者：Stephanie Wickham、Nicholas Regan、Matthew B. West、Vidya Prasanna Kumar、Justin Thai、Pui Kai Li、Paul F. Cook、Marie H. Hanigan

  DOI：10.3109/14756366.2011.597748

  日期：2012.8.1

  A novel class of inhibitors of the enzyme gamma-glutamyl transpeptidase (GGT) were evaluated. The analog OU749 was shown previously to be an uncompetitive inhibitor of the GGT transpeptidation reaction. The data in this study show that it is an equally potent uncompetitive inhibitor of the hydrolysis reaction, the primary reaction catalyzed by GGT in vivo. A series of structural analogs of OU749 were evaluated. For many of the analogs, the potency of the inhibition differed between the hydrolysis and transpeptidation reactions, providing insight into the malleability of the active site of the enzyme. Analogs with electron withdrawing groups on the benzosulfonamide ring, accelerated the hydrolysis reaction, but inhibited the transpeptidation reaction by competing with a dipeptide acceptor. Several of the OU749 analogs inhibited the transpeptidation reaction by slow onset kinetics, similar to acivicin. Further development of inhibitors of the GGT hydrolysis reaction is necessary to provide new therapeutic compounds.