germacrene D

• 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: germacrene D
• 英文别名: (8R)-1-methyl-5-methylidene-8-propan-2-ylcyclodeca-1,6-diene
• 化学式: C₁₅H₂₄
• 分子量: 204.356
• InChiKey: GAIBLDCXCZKKJE-OAHLLOKOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.7
• 重原子数：
  15
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.6
• 拓扑面积：
  0
• 氢给体数：
  0
• 氢受体数：
  0

反应信息

• 作为产物：
  描述：

  法尼基二磷酸-三铵盐 在 (+)-germacrene D synthase from Solidago canadensis 作用下， 生成 germacrene D
  参考文献：
  名称：

  NMR for direct determination of Km and Vmax of enzyme reactions based on the Lambert W function-analysis of progress curves

  摘要：

  H-1 NMR spectroscopy was used to follow the cleavage of sucrose by invertase. The parameters of the enzyme's kinetics, K-m and V-max, were directly determined from progress curves at only one concentration of the substrate. For comparison with the classical Michaelis-Menten analysis, the reaction progress was also monitored at various initial concentrations of 3.5 to 41.8 mM. Using the lambert W function the parameters K-m and V-max were fitted to obtain the experimental progress curve and resulted in K-m = 28 mM and V-max = 13 mu M/s. The result is almost identical to an initial rate analysis that, however, costs much more time and experimental effort. The effect of product inhibition was also investigated. Furthermore, we analyzed a much more complex reaction, the conversion of farnesyl diphosphate into (+)-germacrene D by the enzyme germacrene D synthase, yielding K-m = 379 mu M and k(cat) = 0.04s(-1). The reaction involves an amphiphilic substrate forming micelles and a water insoluble product; using proper controls, the conversion can well be analyzed by the progress curve approach using the Lambert W function. (c) 2011 Published by Elsevier B.V.

  DOI：

  10.1016/j.bbapap.2011.10.011

文献信息

• NMR for direct determination of Km and Vmax of enzyme reactions based on the Lambert W function-analysis of progress curves
  作者：Franziska Exnowitz、Bernd Meyer、Thomas Hackl

  DOI：10.1016/j.bbapap.2011.10.011

  日期：2012.3

  H-1 NMR spectroscopy was used to follow the cleavage of sucrose by invertase. The parameters of the enzyme's kinetics, K-m and V-max, were directly determined from progress curves at only one concentration of the substrate. For comparison with the classical Michaelis-Menten analysis, the reaction progress was also monitored at various initial concentrations of 3.5 to 41.8 mM. Using the lambert W function the parameters K-m and V-max were fitted to obtain the experimental progress curve and resulted in K-m = 28 mM and V-max = 13 mu M/s. The result is almost identical to an initial rate analysis that, however, costs much more time and experimental effort. The effect of product inhibition was also investigated. Furthermore, we analyzed a much more complex reaction, the conversion of farnesyl diphosphate into (+)-germacrene D by the enzyme germacrene D synthase, yielding K-m = 379 mu M and k(cat) = 0.04s(-1). The reaction involves an amphiphilic substrate forming micelles and a water insoluble product; using proper controls, the conversion can well be analyzed by the progress curve approach using the Lambert W function. (c) 2011 Published by Elsevier B.V.