(+)-(1R)-4-methyl-3-cyclohexen-1-yl 4-methylbenzenesulfonate | 141483-99-0

• 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: (+)-(1R)-4-methyl-3-cyclohexen-1-yl 4-methylbenzenesulfonate
• 英文别名: [(1R)-4-methylcyclohex-3-en-1-yl] 4-methylbenzenesulfonate
• CAS: 141483-99-0
• 化学式: C₁₄H₁₈O₃S
• 分子量: 266.361
• InChiKey: UXLGTZDRXIVOMH-ZDUSSCGKSA-N

物化性质

• 沸点：
  391.9±31.0 °C(Predicted)
• 密度：
  1.20±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  18
• 可旋转键数：
  3
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  51.8
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (+)-(1R)-4-methyl-3-cyclohexen-1-yl 4-methylbenzenesulfonate 在 lithium aluminium tetrahydride 作用下， 以 乙醚 、 N,N-二甲基甲酰胺 为溶剂， 反应 9.0h， 生成 4-methylcyclohex-3-en-1-ol
  参考文献：
  名称：

  Trichodiene synthase. Synergistic inhibition by inorganic pyrophosphate and aza analogs of the bisabolyl cation.

  摘要：

  A series of aza analogs of the bisabolyl and alpha-terpinyl cations were tested as inhibitors of the sesquiterpene cyclase, trichodiene synthase. Both (R)- and (S)-16 and (R)- and (S)-13 as well as trimethylamine were only weak inhibitors when incubated alone. In the presence of inorganic pyrophosphate, itself a known competitive inhibitor of trichodiene synthase, all five amines showed strong cooperative competitive inhibition with an enhancement factor estimated to be 10-40. The apparent induced inhibition constant alpha-K(j) decreased in going from trimethylamine to the monoterpene analogs 13 and was strongest for the sesquiterpene analogs 16, indicating that both electrostatic and hydrophobic interactions are important in the binding of each intermediate analog. The cyclase showed little discrimination, however, between the individual enantiomers of each inhibitor.

  DOI：

  10.1021/jo00038a040
• 作为产物：
  描述：

  (+)-(1R)-4-methyl-1-acetoxy-3-cyclohexene 在 吡啶 、 lithium aluminium tetrahydride 作用下， 以 乙醚 为溶剂， 反应 9.5h， 生成 (+)-(1R)-4-methyl-3-cyclohexen-1-yl 4-methylbenzenesulfonate
  参考文献：
  名称：

  Trichodiene synthase. Synergistic inhibition by inorganic pyrophosphate and aza analogs of the bisabolyl cation.

  摘要：

  A series of aza analogs of the bisabolyl and alpha-terpinyl cations were tested as inhibitors of the sesquiterpene cyclase, trichodiene synthase. Both (R)- and (S)-16 and (R)- and (S)-13 as well as trimethylamine were only weak inhibitors when incubated alone. In the presence of inorganic pyrophosphate, itself a known competitive inhibitor of trichodiene synthase, all five amines showed strong cooperative competitive inhibition with an enhancement factor estimated to be 10-40. The apparent induced inhibition constant alpha-K(j) decreased in going from trimethylamine to the monoterpene analogs 13 and was strongest for the sesquiterpene analogs 16, indicating that both electrostatic and hydrophobic interactions are important in the binding of each intermediate analog. The cyclase showed little discrimination, however, between the individual enantiomers of each inhibitor.

  DOI：

  10.1021/jo00038a040

文献信息

• Trichodiene synthase. Synergistic inhibition by inorganic pyrophosphate and aza analogs of the bisabolyl cation.
  作者：David E. Cane、Guohan Yang、Robert M. Coates、Hyung Jung Pyun、Thomas M. Hohn

  DOI：10.1021/jo00038a040

  日期：1992.6

  A series of aza analogs of the bisabolyl and alpha-terpinyl cations were tested as inhibitors of the sesquiterpene cyclase, trichodiene synthase. Both (R)- and (S)-16 and (R)- and (S)-13 as well as trimethylamine were only weak inhibitors when incubated alone. In the presence of inorganic pyrophosphate, itself a known competitive inhibitor of trichodiene synthase, all five amines showed strong cooperative competitive inhibition with an enhancement factor estimated to be 10-40. The apparent induced inhibition constant alpha-K(j) decreased in going from trimethylamine to the monoterpene analogs 13 and was strongest for the sesquiterpene analogs 16, indicating that both electrostatic and hydrophobic interactions are important in the binding of each intermediate analog. The cyclase showed little discrimination, however, between the individual enantiomers of each inhibitor.