7-(2,6-dimethyl-8-hydroxy-2,6-octadienyloxy)-8-methyl-4-trifluoromethyl-chromen-2-one | 489421-44-5

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: 7-(2,6-dimethyl-8-hydroxy-2,6-octadienyloxy)-8-methyl-4-trifluoromethyl-chromen-2-one
• 英文别名: 7-[(2E,6E)-8-hydroxy-2,6-dimethylocta-2,6-dienoxy]-8-methyl-4-(trifluoromethyl)chromen-2-one
• CAS: 489421-44-5
• 化学式: C₂₁H₂₃F₃O₄
• 分子量: 396.406
• InChiKey: RDQPIJXQJAMPRV-WSPXSRFVSA-N

物化性质

• 沸点：
  512.4±50.0 °C(Predicted)
• 密度：
  1.233±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.8
• 重原子数：
  28
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  55.8
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  7-(2,6-dimethyl-8-hydroxy-2,6-octadienyloxy)-8-methyl-4-trifluoromethyl-chromen-2-one 在 四溴化碳 、 三苯基膦 作用下， 以 二氯甲烷 为溶剂， 以80%的产率得到7-(8-bromo-2,6-dimethyl-2,6-octadienyloxy)-8-methyl-4-trifluoromethyl-chromen-2-one
  参考文献：
  名称：

  Synthesis and Application of A Fluorescent Substrate Analogue to Study Ligand Interactions for Undecaprenyl Pyrophosphate Synthase

  摘要：

  Farnesyl pyrophosphate (FPP) serves as a common substrate for many prenyltransferases involved in the biosynthesis of isoprenoid compounds. Undecaprenyl pyrophosphate synthase (UPPs) catalyzes the chain elongation of FPP to C-55 undecaprenyl pyrophosphate (UPP) which acts as a lipid carrier in bacterial peptidoglycan synthesis. In this study, 7-(2,6-dimethyl-8-diphospho-2,6-octadienyloxy)8-methyl-4-trifluoromethyl-chromen-2-one geranyl pyrophosphate, a fluorescent analogue of FPP, was prepared and utilized to study ligand interactions with E coli UPPs. This compound displays an absorbance maximum at 336 nm and emission maximum at 460 nm without interference from protein autofluorescence. It is a competitive inhibitor with respect to FPP (K-i = 0.57 uM) and also serves as an alternative substrate (K-m = 0.69 muM and k(cat) = 0.02 s(-1)), but mainly reacts with one isopentenyl pyrophosphate (IPP) probably due to unfavorable product translocation. Fluorescence intensity of this compound is reduced when bound to the enzyme (1:1 stoichiometry), and is recovered by FPP replacement. Using stopped-flow apparatus, the interaction of enzyme with the compound was measured (k(on) = 55.3 muM(-1) s(-1) and k(off) = 31.6 s(-1)). The product dissociation rate constant (0.5 s(-1)) determined from the competition experiments is consistent with our previous prediction from kinetic simulation. Unlike several other prenyltransferase reactions in which FPP dissociates slowly, UPPs binds FPP in a rapid equilibrium manner with a fast release rate constant of 30 s-1. The fluorescent analogue of FPP presented here may provide a tool to investigate the ligand interactions for a broad class of FPP-binding proteins.

  DOI：

  10.1021/ja020937v
• 作为产物：
  描述：

  2-<(2E,6E)-8-bromo-3,7-dimethylocta-2,6-dien-1-yloxy>tetrahydro-2H-pyran 在 4-甲基苯磺酸吡啶 、 potassium carbonate 作用下， 以 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 12.0h， 生成 7-(2,6-dimethyl-8-hydroxy-2,6-octadienyloxy)-8-methyl-4-trifluoromethyl-chromen-2-one
  参考文献：
  名称：

  Synthesis and Application of A Fluorescent Substrate Analogue to Study Ligand Interactions for Undecaprenyl Pyrophosphate Synthase

  摘要：

  Farnesyl pyrophosphate (FPP) serves as a common substrate for many prenyltransferases involved in the biosynthesis of isoprenoid compounds. Undecaprenyl pyrophosphate synthase (UPPs) catalyzes the chain elongation of FPP to C-55 undecaprenyl pyrophosphate (UPP) which acts as a lipid carrier in bacterial peptidoglycan synthesis. In this study, 7-(2,6-dimethyl-8-diphospho-2,6-octadienyloxy)8-methyl-4-trifluoromethyl-chromen-2-one geranyl pyrophosphate, a fluorescent analogue of FPP, was prepared and utilized to study ligand interactions with E coli UPPs. This compound displays an absorbance maximum at 336 nm and emission maximum at 460 nm without interference from protein autofluorescence. It is a competitive inhibitor with respect to FPP (K-i = 0.57 uM) and also serves as an alternative substrate (K-m = 0.69 muM and k(cat) = 0.02 s(-1)), but mainly reacts with one isopentenyl pyrophosphate (IPP) probably due to unfavorable product translocation. Fluorescence intensity of this compound is reduced when bound to the enzyme (1:1 stoichiometry), and is recovered by FPP replacement. Using stopped-flow apparatus, the interaction of enzyme with the compound was measured (k(on) = 55.3 muM(-1) s(-1) and k(off) = 31.6 s(-1)). The product dissociation rate constant (0.5 s(-1)) determined from the competition experiments is consistent with our previous prediction from kinetic simulation. Unlike several other prenyltransferase reactions in which FPP dissociates slowly, UPPs binds FPP in a rapid equilibrium manner with a fast release rate constant of 30 s-1. The fluorescent analogue of FPP presented here may provide a tool to investigate the ligand interactions for a broad class of FPP-binding proteins.

  DOI：

  10.1021/ja020937v

文献信息

• Synthesis and Application of A Fluorescent Substrate Analogue to Study Ligand Interactions for Undecaprenyl Pyrophosphate Synthase
  作者：Annie P.-C. Chen、Yi-Hung Chen、Hsiao-Pei Liu、Yu-Chin Li、Chao-Tsen Chen、Po-Huang Liang

  DOI：10.1021/ja020937v

  日期：2002.12.1

  Farnesyl pyrophosphate (FPP) serves as a common substrate for many prenyltransferases involved in the biosynthesis of isoprenoid compounds. Undecaprenyl pyrophosphate synthase (UPPs) catalyzes the chain elongation of FPP to C-55 undecaprenyl pyrophosphate (UPP) which acts as a lipid carrier in bacterial peptidoglycan synthesis. In this study, 7-(2,6-dimethyl-8-diphospho-2,6-octadienyloxy)8-methyl-4-trifluoromethyl-chromen-2-one geranyl pyrophosphate, a fluorescent analogue of FPP, was prepared and utilized to study ligand interactions with E coli UPPs. This compound displays an absorbance maximum at 336 nm and emission maximum at 460 nm without interference from protein autofluorescence. It is a competitive inhibitor with respect to FPP (K-i = 0.57 uM) and also serves as an alternative substrate (K-m = 0.69 muM and k(cat) = 0.02 s(-1)), but mainly reacts with one isopentenyl pyrophosphate (IPP) probably due to unfavorable product translocation. Fluorescence intensity of this compound is reduced when bound to the enzyme (1:1 stoichiometry), and is recovered by FPP replacement. Using stopped-flow apparatus, the interaction of enzyme with the compound was measured (k(on) = 55.3 muM(-1) s(-1) and k(off) = 31.6 s(-1)). The product dissociation rate constant (0.5 s(-1)) determined from the competition experiments is consistent with our previous prediction from kinetic simulation. Unlike several other prenyltransferase reactions in which FPP dissociates slowly, UPPs binds FPP in a rapid equilibrium manner with a fast release rate constant of 30 s-1. The fluorescent analogue of FPP presented here may provide a tool to investigate the ligand interactions for a broad class of FPP-binding proteins.