N-methyl-5-(4-benzyloxybenzylidene)-2-thiobarbituric acid | 1402934-19-3

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: N-methyl-5-(4-benzyloxybenzylidene)-2-thiobarbituric acid
• 英文别名: 1-methyl-5-[(4-phenylmethoxyphenyl)methylidene]-2-sulfanylidene-1,3-diazinane-4,6-dione
• CAS: 1402934-19-3
• 化学式: C₁₉H₁₆N₂O₃S
• 分子量: 352.414
• InChiKey: HRVBHCYNMJPPFC-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.52
• 重原子数：
  25.0
• 可旋转键数：
  4.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  58.64
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为产物：
  描述：

  4-苄氧基苯甲醛 、 1-methyl-2-thioxodihydropyrimidine-4,6(1H,5H)-dione 在 盐酸 作用下， 以 乙醇 为溶剂， 以51%的产率得到N-methyl-5-(4-benzyloxybenzylidene)-2-thiobarbituric acid
  参考文献：
  名称：

  Inhibitors of the NAD⁺-Dependent Protein Desuccinylase and Demalonylase Sirt5

  摘要：

  NAD(+)-dependent histone deacetylases (sirtuins) play important roles in epigenetic regulation but also through nonhistone substrates for other key cellular events and have been linked to the pathogenesis of cancer, neuro-degeneration, and metabolic diseases. The subtype Sirt5 has been shown recently to act as a desuccinylating and demalonylating enzyme. We have established an assay for biochemical testing of Sirt5 using a small labeled succinylated lysine derivative. We present a comparative study on the profiling of several established sirtuin inhibitors on Sirt1-3 as well as Sirt5 and also present initial results on a screening for new compounds that block Sirt5. Thiobarbiturates were identified as new Sirt5 inhibitors in the low micromolar range, which are selective over Sirt3 that can be found in the same cell compartment as Sirt5.

  DOI：

  10.1021/ml3002709

文献信息

• Inhibitors of the NAD⁺-Dependent Protein Desuccinylase and Demalonylase Sirt5
  作者：Benjamin Maurer、Tobias Rumpf、Michael Scharfe、Diana A. Stolfa、Martin L. Schmitt、Wenjuan He、Eric Verdin、Wolfgang Sippl、Manfred Jung

  DOI：10.1021/ml3002709

  日期：2012.12.13

  NAD(+)-dependent histone deacetylases (sirtuins) play important roles in epigenetic regulation but also through nonhistone substrates for other key cellular events and have been linked to the pathogenesis of cancer, neuro-degeneration, and metabolic diseases. The subtype Sirt5 has been shown recently to act as a desuccinylating and demalonylating enzyme. We have established an assay for biochemical testing of Sirt5 using a small labeled succinylated lysine derivative. We present a comparative study on the profiling of several established sirtuin inhibitors on Sirt1-3 as well as Sirt5 and also present initial results on a screening for new compounds that block Sirt5. Thiobarbiturates were identified as new Sirt5 inhibitors in the low micromolar range, which are selective over Sirt3 that can be found in the same cell compartment as Sirt5.