5-ethynyl-1-pentylpyridin-2(1H)-one | 1357170-91-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡啶及其衍生物
• 英文名称: 5-ethynyl-1-pentylpyridin-2(1H)-one
• 英文别名: 5-Ethynyl-1-pentylpyridin-2-one
• CAS: 1357170-91-2
• 化学式: C₁₂H₁₅NO
• 分子量: 189.257
• InChiKey: GHEMFMUJRIFJOP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  14
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  20.3
• 氢给体数：
  0
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  5-ethynyl-1-pentylpyridin-2(1H)-one 在 bis-triphenylphosphine-palladium(II) chloride 、 copper(l) iodide 、 palladium 10% on activated carbon 、 氢气 、 二乙胺 作用下， 以 甲醇 、 乙腈 为溶剂， 40.0~100.0 ℃ 、303.99 kPa 条件下， 反应 0.5h， 生成 5-(2-(2,2-dimethyl-4-oxo-4H-benzo[d][1,3]dioxin-5-yl)ethyl)-1-pentylpiperidin-2-one
  参考文献：
  名称：

  6-alkylsalicylates are selective Tip60 inhibitors and target the acetyl-CoA binding site

  摘要：

  Histone acetyltransferases are important enzymes that regulate various cellular functions, such as epigenetic control of DNA transcription. Development of HAT inhibitors with high selectivity and potency will provide powerful mechanistic tools for the elucidation of the biological functions of HATs and may also have pharmacological value for potential new therapies. In this work, analogs of the known HAT inhibitor anacardic acid were synthesized and evaluated for inhibition of HAT activity. Biochemical assays revealed novel anacardic acid analogs that inhibited the human recombinant enzyme Tip60 selectively compared to PCAF and p300. Enzyme kinetics studies demonstrated that inhibition of Tip60 by one such novel anacardic acid derive, 20, was essentially competitive with Ac-CoA and non-competitive with the histone substrate. In addition, these HAT inhibitors effectively inhibited acetyltransferase activity of nuclear extracts on the histone H3 and H4 at micromolar concentrations. (C) 2011 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2011.11.001
• 作为产物：
  描述：

  2-羟基-5-溴吡啶 在 bis-triphenylphosphine-palladium(II) chloride 、 copper(l) iodide 、 四丁基氟化铵 、 potassium carbonate 、 二乙胺 、 三苯基膦 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 1.0h， 生成 5-ethynyl-1-pentylpyridin-2(1H)-one
  参考文献：
  名称：

  6-alkylsalicylates are selective Tip60 inhibitors and target the acetyl-CoA binding site

  摘要：

  Histone acetyltransferases are important enzymes that regulate various cellular functions, such as epigenetic control of DNA transcription. Development of HAT inhibitors with high selectivity and potency will provide powerful mechanistic tools for the elucidation of the biological functions of HATs and may also have pharmacological value for potential new therapies. In this work, analogs of the known HAT inhibitor anacardic acid were synthesized and evaluated for inhibition of HAT activity. Biochemical assays revealed novel anacardic acid analogs that inhibited the human recombinant enzyme Tip60 selectively compared to PCAF and p300. Enzyme kinetics studies demonstrated that inhibition of Tip60 by one such novel anacardic acid derive, 20, was essentially competitive with Ac-CoA and non-competitive with the histone substrate. In addition, these HAT inhibitors effectively inhibited acetyltransferase activity of nuclear extracts on the histone H3 and H4 at micromolar concentrations. (C) 2011 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2011.11.001

文献信息

• 6-alkylsalicylates are selective Tip60 inhibitors and target the acetyl-CoA binding site
  作者：Massimo Ghizzoni、Jiang Wu、Tielong Gao、Hidde J. Haisma、Frank J. Dekker、Y. George Zheng

  DOI：10.1016/j.ejmech.2011.11.001

  日期：2012.1

  Histone acetyltransferases are important enzymes that regulate various cellular functions, such as epigenetic control of DNA transcription. Development of HAT inhibitors with high selectivity and potency will provide powerful mechanistic tools for the elucidation of the biological functions of HATs and may also have pharmacological value for potential new therapies. In this work, analogs of the known HAT inhibitor anacardic acid were synthesized and evaluated for inhibition of HAT activity. Biochemical assays revealed novel anacardic acid analogs that inhibited the human recombinant enzyme Tip60 selectively compared to PCAF and p300. Enzyme kinetics studies demonstrated that inhibition of Tip60 by one such novel anacardic acid derive, 20, was essentially competitive with Ac-CoA and non-competitive with the histone substrate. In addition, these HAT inhibitors effectively inhibited acetyltransferase activity of nuclear extracts on the histone H3 and H4 at micromolar concentrations. (C) 2011 Elsevier Masson SAS. All rights reserved.