1-hydroxy-3-N-n-octylcarbamyloxybenzene | 900494-86-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 1-hydroxy-3-N-n-octylcarbamyloxybenzene
• CAS: 900494-86-2
• 化学式: C₁₅H₂₃NO₃
• 分子量: 265.353
• InChiKey: OPPQHJVZBJIKSN-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.84
• 重原子数：
  19.0
• 可旋转键数：
  8.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  58.56
• 氢给体数：
  2.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  1-hydroxy-3-N-n-octylcarbamyloxybenzene 、 三氯乙酰氯 在 三乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 24.0h， 生成 Trichloro-acetic acid 3-octylcarbamoyloxy-phenyl ester
  参考文献：
  名称：

  QSAR for phospholipase A2 inhibitions by 1-acyloxy-3-N-n-octylcarbamyl-benzenes

  摘要：

  1-Acyloxy-3-N-n-octylcarbamyl-benzenes are potent reversible competitive inhibitors of Naja mocambique mocambique phospholipase A(2) with the K-i values from 9.6 to 119 μ M. The pK(i) values are correlated to both Taft substituent constant σ(*) and Hansch hydrophobicity constant π. The pre-steady state inhibition studies indicate that the pK(s) values for the first inhibition step are linearly correlated to σ(*) alone with the p(*) of -0.09 for this correlation. Thus, the first inhibition step may involve the insertion of the inhibitor to hepta-coordinated Ca2+ ion of the enzyme to form the octa-coordinated Ca2+ ion of the enzyme. The log(k(2)/k(-2)) values for the second inhibition step are linearly correlated to 71 alone, and the ψ value for this correlation is 0.13. Therefore, the second step inhibition step may involve the van der Waals' interaction between the acyl group of the inhibitor and Tyr 69 of the enzyme. © 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2005.02.092
• 作为产物：
  描述：

  正辛基异氰酸酯 、 间苯二酚 在 三乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 24.0h， 生成 1-hydroxy-3-N-n-octylcarbamyloxybenzene
  参考文献：
  名称：

  QSAR for phospholipase A2 inhibitions by 1-acyloxy-3-N-n-octylcarbamyl-benzenes

  摘要：

  1-Acyloxy-3-N-n-octylcarbamyl-benzenes are potent reversible competitive inhibitors of Naja mocambique mocambique phospholipase A(2) with the K-i values from 9.6 to 119 μ M. The pK(i) values are correlated to both Taft substituent constant σ(*) and Hansch hydrophobicity constant π. The pre-steady state inhibition studies indicate that the pK(s) values for the first inhibition step are linearly correlated to σ(*) alone with the p(*) of -0.09 for this correlation. Thus, the first inhibition step may involve the insertion of the inhibitor to hepta-coordinated Ca2+ ion of the enzyme to form the octa-coordinated Ca2+ ion of the enzyme. The log(k(2)/k(-2)) values for the second inhibition step are linearly correlated to 71 alone, and the ψ value for this correlation is 0.13. Therefore, the second step inhibition step may involve the van der Waals' interaction between the acyl group of the inhibitor and Tyr 69 of the enzyme. © 2005 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2005.02.092