sodium;1-ethoxy-5-ethyl-1,4-dioxohept-2-en-2-olate | 1436852-31-1

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: sodium;1-ethoxy-5-ethyl-1,4-dioxohept-2-en-2-olate
• CAS: 1436852-31-1
• 化学式: C₁₁H₁₇O₄*Na
• 分子量: 236.243
• InChiKey: JYAOVLLYZALUMT-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -2.2
• 重原子数：
  16.0
• 可旋转键数：
  6.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  66.43
• 氢给体数：
  0.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  sodium;1-ethoxy-5-ethyl-1,4-dioxohept-2-en-2-olate 在 一水合肼 作用下， 以 乙醇 为溶剂， 以98%的产率得到ethyl 5-pentan-3-yl-1H-pyrazole-3-carboxylate
  参考文献：
  名称：

  Discovery of potent, selective, bioavailable phosphodiesterase 2 (PDE2) inhibitors active in an osteoarthritis pain model, Part I: Transformation of selective pyrazolodiazepinone phosphodiesterase 4 (PDE4) inhibitors into selective PDE2 inhibitors

  摘要：

  We identified potent, selective PDE2 inhibitors by optimizing residual PDE2 activity in a series of PDE4 inhibitors, while simultaneously minimizing PDE4 activity. These newly designed PDE2 inhibitors bind to the PDE2 enzyme in a cGMP-like mode in contrast to the cAMP-like binding mode found in PDE4. Structure activity relationship studies coupled with an inhibitor bound crystal structure in the active site of the catalytic domain of PDE2 identified structural features required to minimize PDE4 inhibition while simultaneously maximizing PDE2 inhibition. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.03.072
• 作为产物：
  描述：

  3-乙基-2-戊酮 、 草酸二乙酯 在 sodium ethanolate 作用下， 以 乙醇 为溶剂， 以72%的产率得到sodium;1-ethoxy-5-ethyl-1,4-dioxohept-2-en-2-olate
  参考文献：
  名称：

  Discovery of potent, selective, bioavailable phosphodiesterase 2 (PDE2) inhibitors active in an osteoarthritis pain model, Part I: Transformation of selective pyrazolodiazepinone phosphodiesterase 4 (PDE4) inhibitors into selective PDE2 inhibitors

  摘要：

  We identified potent, selective PDE2 inhibitors by optimizing residual PDE2 activity in a series of PDE4 inhibitors, while simultaneously minimizing PDE4 activity. These newly designed PDE2 inhibitors bind to the PDE2 enzyme in a cGMP-like mode in contrast to the cAMP-like binding mode found in PDE4. Structure activity relationship studies coupled with an inhibitor bound crystal structure in the active site of the catalytic domain of PDE2 identified structural features required to minimize PDE4 inhibition while simultaneously maximizing PDE2 inhibition. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.03.072