7-oxo-oxepan-4-carboxylic acid ethyl ester | 915092-90-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 内酯类
• 英文名称: 7-oxo-oxepan-4-carboxylic acid ethyl ester
• 英文别名: ethyl (4S)-7-oxooxepane-4-carboxylate
• CAS: 915092-90-9
• 化学式: C₉H₁₄O₄
• 分子量: 186.208
• InChiKey: MEYMFRXJFXOZHU-ZETCQYMHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  13
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  52.6
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  7-oxo-oxepan-4-carboxylic acid ethyl ester 在 lithium aluminium tetrahydride 作用下， 以 四氢呋喃 为溶剂， 反应 7.5h， 以39%的产率得到(S)-3-hydroxymethylhexane-1,6-diol
  参考文献：
  名称：

  New Bioorganic Reagents:  Evolved Cyclohexanone MonooxygenaseWhy Is It More Selective?

  摘要：

  Four mutants of the cyclohexanone monooxygenase (CHMO) evolved as catalysts for Baeyer-Villiger oxidation of 4-hydroxycyclohexanone were investigated as catalysts for a variety of 4-substituted and 4,4-disubstituted cyclohexanones. Several excellent catalytic matches (mutant/substrate) were identified. The most important, however, is the finding that, in a number of cases, a mutant with a single exchange, Phe432Ser, was shown to be as robust and more selective as a catalyst than the wild-type CHMO. All biotransformations were performed on a laboratory scale, allowing full characterization of the products. The absolute configurations of two products were established. A model suggesting a possible role of the 432 serine residue in enantioselectivity control is proposed.

  DOI：

  10.1021/jo061349t
• 作为产物：
  描述：

  对环己酮甲酸乙酯 在 葡萄糖 Escherichia coli JM₁₀₉(DE₃)(pET-22b) whole cells 、 LB-Ampicillin medium 、 异丙基-beta-D-硫代半乳糖吡喃糖苷 作用下， 以 水 为溶剂， 以63%的产率得到7-oxo-oxepan-4-carboxylic acid ethyl ester
  参考文献：
  名称：

  New Bioorganic Reagents:  Evolved Cyclohexanone MonooxygenaseWhy Is It More Selective?

  摘要：

  Four mutants of the cyclohexanone monooxygenase (CHMO) evolved as catalysts for Baeyer-Villiger oxidation of 4-hydroxycyclohexanone were investigated as catalysts for a variety of 4-substituted and 4,4-disubstituted cyclohexanones. Several excellent catalytic matches (mutant/substrate) were identified. The most important, however, is the finding that, in a number of cases, a mutant with a single exchange, Phe432Ser, was shown to be as robust and more selective as a catalyst than the wild-type CHMO. All biotransformations were performed on a laboratory scale, allowing full characterization of the products. The absolute configurations of two products were established. A model suggesting a possible role of the 432 serine residue in enantioselectivity control is proposed.

  DOI：

  10.1021/jo061349t

文献信息

• Self-Sufficient Baeyer–Villiger Monooxygenases: Effective Coenzyme Regeneration for Biooxygenation by Fusion Engineering
  作者：Daniel E. Torres Pazmiño、Radka Snajdrova、Bert-Jan Baas、Michael Ghobrial、Marko D. Mihovilovic、Marco W. Fraaije

  DOI：10.1002/anie.200704630

  日期：2008.3.7
• Increasing the enantioselectivity of cyclopentanone monooxygenase (CPMO): profile of new CPMO mutants
  作者：Christopher M. Clouthier、Margaret M. Kayser

  DOI：10.1016/j.tetasy.2006.10.001

  日期：2006.10

  A series of cyclohexanones substituted at the 4-position with a selection of hydrophobic and hydrophilic groups were used as substrates in the evaluation of six new cyclopentanone monooxygenase (CPMO) mutants. These mutants were obtained through evolutionary modifications in two specific regions of the CPMO's putative active site. Several mutant enzymes with improved enantioselectivity were identified. Analysis of the results, in terms of a diamond model, illustrates how a family of cyclohexanone substrates may be used to explore putative active sites of Baeyer-Villiger monooxygenases (BVMOs) and to design productive mutations for specific substrates. (c) 2006 Elsevier Ltd. All rights reserved.
• New Bioorganic Reagents:  Evolved Cyclohexanone MonooxygenaseWhy Is It More Selective?
  作者：Margaret M. Kayser、Christopher M. Clouthier

  DOI：10.1021/jo061349t

  日期：2006.10.1

  Four mutants of the cyclohexanone monooxygenase (CHMO) evolved as catalysts for Baeyer-Villiger oxidation of 4-hydroxycyclohexanone were investigated as catalysts for a variety of 4-substituted and 4,4-disubstituted cyclohexanones. Several excellent catalytic matches (mutant/substrate) were identified. The most important, however, is the finding that, in a number of cases, a mutant with a single exchange, Phe432Ser, was shown to be as robust and more selective as a catalyst than the wild-type CHMO. All biotransformations were performed on a laboratory scale, allowing full characterization of the products. The absolute configurations of two products were established. A model suggesting a possible role of the 432 serine residue in enantioselectivity control is proposed.
• Extensive substrate profiling of cyclopentadecanone monooxygenase as Baeyer–Villiger biocatalyst reveals novel regiodivergent oxidations
  作者：Michael J. Fink、Thomas C. Fischer、Florian Rudroff、Hanna Dudek、Marco W. Fraaije、Marko D. Mihovilovic

  DOI：10.1016/j.molcatb.2011.07.003

  日期：2011.12

  Cyclopentadecanone monooxygenase (CPDMO) is one of the latest additions to the established library of Baeyer-Villiger monooxygenases. Desymmetrizations of substituted cyclobutanones and -hexanones as well as kinetic resolutions of racemic cycloketones are efficiently catalyzed by CPDMO. Moreover the enzyme shows unprecedented preference in regiodivergent oxidations of terpenones and the bicyclic Geissman-Waiss lactone precursor giving access to the optical antipode of retronecine and other pyrrolizidine alkaloids. (C) 2011 Elsevier B.V. All rights reserved.