methyl 2,4-dihydroxy-6-methyl-3-[(E)-3-methyl-5-[(1S,2R,6R)-1,2,6-trimethyl-3-oxocyclohexyl]pent-2-enyl]benzoate | 165187-10-0

• 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: methyl 2,4-dihydroxy-6-methyl-3-[(E)-3-methyl-5-[(1S,2R,6R)-1,2,6-trimethyl-3-oxocyclohexyl]pent-2-enyl]benzoate
• CAS: 165187-10-0
• 化学式: C₂₄H₃₄O₅
• 分子量: 402.531
• InChiKey: SEQMTELCJHGFIO-ABGOUHDQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.2
• 重原子数：
  29
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  83.8
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  methyl 2,4-dihydroxy-6-methyl-3-[(E)-3-methyl-5-[(1S,2R,6R)-1,2,6-trimethyl-3-oxocyclohexyl]pent-2-enyl]benzoate 在 sodium hydroxide 作用下， 以 四氢呋喃 、 甲醇 为溶剂， 以0.7 mg的产率得到(2R,3S,4R)-3-[(E)-5-(2,6-dihydroxy-4-methylphenyl)-3-methylpent-3-enyl]-2,3,4-trimethylcyclohexan-1-one
  参考文献：
  名称：

  Chemistry and Biology of Cylindrols:  Novel Inhibitors of Ras Farnesyl-Protein Transferase from Cylindrocarpon lucidum

  摘要：

  Farnesyl-protein transferase (FPTase) is an enzyme responsible for the farnesylation of Ras protein. Farnesylation is required for cell-transforming activity in several tumor-types, and therefore, inhibition of FPTase activity may be a potential target for anticancer drugs. Our continued search for novel inhibitors led to the isolation of a number of bicyclic resorcinaldehyde cyclohexanone derivatives named here cylindrols A(1) to A(4), cylindrols B and B-1, and a number of known compounds, from Cylindrocarpon Lucidum. The compounds were isolated by bioassay-guided separation using Sephadex LH-20, silica gel, and reverse phase HPLC. Structures were elucidated by extensive application of 2D NMR and X-ray crystallography. The determination of absolute stereochemistry was accomplished by CD measurements. Chemical transformations of the most abundant compound resulted in a number of key derivatives which were critical for the evaluation of structure activity relationship. These compounds are members of ascochlorin family and showed a wide range of inhibitory activity (0.7 mu M to > 140 mu M) against FPTase. The FPTase activity was noncompetitive with respect to both substrates. Isolation, structures, chemical transformations, and FPTase activity are discussed in detail.

  DOI：

  10.1021/jo961074p
• 作为产物：
  描述：

  甲醇 、 LL-Z 1272ε 在 potassium cyanide 、 manganese(IV) oxide 、 溶剂黄146 作用下， 以60 mg的产率得到methyl 2,4-dihydroxy-6-methyl-3-[(E)-3-methyl-5-[(1S,2R,6R)-1,2,6-trimethyl-3-oxocyclohexyl]pent-2-enyl]benzoate
  参考文献：
  名称：

  Chemistry and Biology of Cylindrols:  Novel Inhibitors of Ras Farnesyl-Protein Transferase from Cylindrocarpon lucidum

  摘要：

  Farnesyl-protein transferase (FPTase) is an enzyme responsible for the farnesylation of Ras protein. Farnesylation is required for cell-transforming activity in several tumor-types, and therefore, inhibition of FPTase activity may be a potential target for anticancer drugs. Our continued search for novel inhibitors led to the isolation of a number of bicyclic resorcinaldehyde cyclohexanone derivatives named here cylindrols A(1) to A(4), cylindrols B and B-1, and a number of known compounds, from Cylindrocarpon Lucidum. The compounds were isolated by bioassay-guided separation using Sephadex LH-20, silica gel, and reverse phase HPLC. Structures were elucidated by extensive application of 2D NMR and X-ray crystallography. The determination of absolute stereochemistry was accomplished by CD measurements. Chemical transformations of the most abundant compound resulted in a number of key derivatives which were critical for the evaluation of structure activity relationship. These compounds are members of ascochlorin family and showed a wide range of inhibitory activity (0.7 mu M to > 140 mu M) against FPTase. The FPTase activity was noncompetitive with respect to both substrates. Isolation, structures, chemical transformations, and FPTase activity are discussed in detail.

  DOI：

  10.1021/jo961074p

文献信息

• Chemistry and Biology of Cylindrols:  Novel Inhibitors of Ras Farnesyl-Protein Transferase from <i>Cylindrocarpon lucidum</i>
  作者：Sheo B. Singh、Richard G. Ball、Gerald F. Bills、Carmen Cascales、Jackson B. Gibbs、Michael A. Goetz、Karst Hoogsteen、Rosalind G. Jenkins、Jerrold M. Liesch、Russell B. Lingham、Keith C. Silverman、Deborah L. Zink

  DOI：10.1021/jo961074p

  日期：1996.1.1

  Farnesyl-protein transferase (FPTase) is an enzyme responsible for the farnesylation of Ras protein. Farnesylation is required for cell-transforming activity in several tumor-types, and therefore, inhibition of FPTase activity may be a potential target for anticancer drugs. Our continued search for novel inhibitors led to the isolation of a number of bicyclic resorcinaldehyde cyclohexanone derivatives named here cylindrols A(1) to A(4), cylindrols B and B-1, and a number of known compounds, from Cylindrocarpon Lucidum. The compounds were isolated by bioassay-guided separation using Sephadex LH-20, silica gel, and reverse phase HPLC. Structures were elucidated by extensive application of 2D NMR and X-ray crystallography. The determination of absolute stereochemistry was accomplished by CD measurements. Chemical transformations of the most abundant compound resulted in a number of key derivatives which were critical for the evaluation of structure activity relationship. These compounds are members of ascochlorin family and showed a wide range of inhibitory activity (0.7 mu M to > 140 mu M) against FPTase. The FPTase activity was noncompetitive with respect to both substrates. Isolation, structures, chemical transformations, and FPTase activity are discussed in detail.