2-Methyl-4-(2,6,6-trimethyl-1-cyclohexen-1-yl)-3-buten-1-ol | 3310-00-7

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 2-Methyl-4-(2,6,6-trimethyl-1-cyclohexen-1-yl)-3-buten-1-ol
• 英文别名: 2-Methyl-4-(2,6,6-trimethylcyclohexen-1-yl)but-3-en-1-ol
• CAS: 3310-00-7
• 化学式: C₁₄H₂₄O
• 分子量: 208.344
• InChiKey: SFPJUSGYMAXMDP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.3
• 重原子数：
  15
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  20.2
• 氢给体数：
  1
• 氢受体数：
  1

反应信息

• 作为产物：
  描述：

  β-胡萝卜素 在 sodium tetrahydroborate 、 carotenoid cleavage dioxygenase CCD₇ 、 carotenoid cleavage dioxygenase CCD₈ 、 cis–trans isomerase Dwarf27 、 水 、 碘 、 氧气 、 iron(II) sulfate 作用下， 以 aq. phosphate buffer 、 正己烷 为溶剂， 反应 0.5h， 生成 2-Methyl-4-(2,6,6-trimethyl-1-cyclohexen-1-yl)-3-buten-1-ol
  参考文献：
  名称：

  Biochemical characterization and selective inhibition of β-carotenecis-transisomerase D27 and carotenoid cleavage dioxygenase CCD8 on the strigolactone biosynthetic pathway

  摘要：

  The first three enzymatic steps of the strigolactone biosynthetic pathway catalysed by β‐carotene cis–trans isomerase Dwarf27 (D27) from Oryza sativa and carotenoid cleavage dioxygenases CCD7 and CCD8 from Arabidopsis thaliana have been reconstituted in vitro, and kinetic assays have been developed for each enzyme, in order to develop selective enzyme inhibitors. Recombinant OsD27 shows a UV‐visible λmax at 422 nm and is inactivated by silver(I) acetate, consistent with the presence of an iron–sulfur cluster that is used in catalysis. OsD27 and AtCCD7 are not inhibited by hydroxamic acids that cause shoot branching in planta, but OsD27 is partially inhibited by terpene‐like hydroxamic acids. The reaction catalysed by AtCCD8 is shown to be a two‐step kinetic mechanism using pre‐steady‐state kinetic analysis. Kinetic evidence is presented for acid–base catalysis in the CCD8 catalytic cycle and the existence of an essential cysteine residue in the CCD8 active site. AtCCD8 is inhibited in a time‐dependent fashion by hydroxamic acids D2, D4, D5 and D6 (> 95% inhibition at 100 μm) that cause a shoot branching phenotype in A. thaliana, and selective inhibition of CCD8 is observed using hydroxamic acids D13H and D15 (82%, 71% inhibition at 10 μm). The enzyme inhibition data imply that the biochemical basis of the shoot branching phenotype is due to inhibition of CCD8.

  DOI：

  10.1111/febs.13400

文献信息

• Biochemical characterization and selective inhibition of β-carotene<i>cis-trans</i>isomerase D27 and carotenoid cleavage dioxygenase CCD8 on the strigolactone biosynthetic pathway
  作者：Peter J. Harrison、Sophie A. Newgas、Flora Descombes、Sarah A. Shepherd、Andrew J. Thompson、Timothy D. H. Bugg

  DOI：10.1111/febs.13400

  日期：2015.10

  The first three enzymatic steps of the strigolactone biosynthetic pathway catalysed by β‐carotene cis–trans isomerase Dwarf27 (D27) from Oryza sativa and carotenoid cleavage dioxygenases CCD7 and CCD8 from Arabidopsis thaliana have been reconstituted in vitro, and kinetic assays have been developed for each enzyme, in order to develop selective enzyme inhibitors. Recombinant OsD27 shows a UV‐visible λmax at 422 nm and is inactivated by silver(I) acetate, consistent with the presence of an iron–sulfur cluster that is used in catalysis. OsD27 and AtCCD7 are not inhibited by hydroxamic acids that cause shoot branching in planta, but OsD27 is partially inhibited by terpene‐like hydroxamic acids. The reaction catalysed by AtCCD8 is shown to be a two‐step kinetic mechanism using pre‐steady‐state kinetic analysis. Kinetic evidence is presented for acid–base catalysis in the CCD8 catalytic cycle and the existence of an essential cysteine residue in the CCD8 active site. AtCCD8 is inhibited in a time‐dependent fashion by hydroxamic acids D2, D4, D5 and D6 (> 95% inhibition at 100 μm) that cause a shoot branching phenotype in A. thaliana, and selective inhibition of CCD8 is observed using hydroxamic acids D13H and D15 (82%, 71% inhibition at 10 μm). The enzyme inhibition data imply that the biochemical basis of the shoot branching phenotype is due to inhibition of CCD8.