(R)-1,3,3-三甲基-2-氧杂双环[2.2.2]辛烷-6-酮 | 70222-88-7

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 氧烷类
• 中文名称: (R)-1,3,3-三甲基-2-氧杂双环[2.2.2]辛烷-6-酮
• 英文名称: (1R)-6-ketocineole
• 英文别名: (1R)-1,8-epoxy-p-menthan-2-one；(1R)-1,8-Epoxy-p-menthan-2-on；6-Oxocineole；(1R,4S)-1,3,3-trimethyl-2-oxabicyclo[2.2.2]octan-6-one
• CAS: 70222-88-7
• 化学式: C₁₀H₁₆O₂
• 分子量: 168.236
• InChiKey: CCBAAZXPXFYPBE-OIBJUYFYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.2
• 重原子数：
  12
• 可旋转键数：
  0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.9
• 拓扑面积：
  26.3
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  (R)-1,3,3-三甲基-2-氧杂双环[2.2.2]辛烷-6-酮 在 selenium(IV) oxide 、 对甲苯磺酸 作用下， 以 溶剂黄146 、 甲苯 为溶剂， 反应 12.4h， 生成 (1R)-5-(1,3-dioxolan-2-yl)-6-ketocineole
  参考文献：
  名称：

  Synthesis of oxygenated cineole derivatives from cineole: utility of cytochrome P450cin as an enantioselective catalyst

  摘要：

  The oxidation of cineole to (1R)-6 beta-hydroxycineole by cytochrome P450(cin) (CYP176A) is utilised as the initial step in the synthesis of a range of compounds, both novel and ones previously known only as race-mates. The potential of P450(cin) to provide useful, enantiopure building blocks is thus demonstrated. In particular, hydroxylation by this enzyme was used as the initial step in the synthesis of a range of functionalised cineole derivatives that could be used as mechanistic probes to elucidate the effect of substrate structure on the transformations mediated by P450(cin). (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2013.02.004
• 作为产物：
  描述：

  (1R)-6β-hydroxycineole 在 (1R)-6β-hydroxycineole dehydrogenase 、 β-烟酰胺腺嘌呤二核苷酸 作用下， 以 乙醇 为溶剂， 生成 (R)-1,3,3-三甲基-2-氧杂双环[2.2.2]辛烷-6-酮
  参考文献：
  名称：

  Cineole biodegradation: Molecular cloning, expression and characterisation of (1R)-6β-hydroxycineole dehydrogenase from Citrobacter braakii

  摘要：

  The first steps in the biodegradation of 1,8-cineole involve the introduction of an alcohol and its subsequent oxidation to a ketone. In Citrobacter braakii, cytochrome P450(cin) has previously been demonstrated to perform the first oxidation to produce (1R)-6 beta-hydroxycineole. In this study, we have cloned cinD from C. braakii and expressed the gene product, which displays significant homology to a number of short-chain alcohol dehydrogenases. It was demonstrated that the gene product of cinD exhibits (1R)-6 beta-hydroxycineole dehydrogenase activity, the second step in the degradation of 1,8-cineole. All four isomers of 6-hydroxycineole were examined but only (1R)-6 beta-hydroxycineole was converted to (1R)-6-ketocineole. The (1R)-6 beta-hydroxycineole dehydrogenase exhibited a strict requirement for NAD(H), with no reaction observed in the presence of NADP(H). The enzyme also catalyses the reverse reaction, reducing (1R)-6-ketocineole to (1R)-6 beta-hydroxycineole. During this study the N-terminal His-tag used to assist protein purification was found to interfere with NAD(H) binding and lower enzyme activity. This could be recovered by the addition of Ni2+ ions or proteolytic removal of the His-tag. (C) 2009 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.bioorg.2009.12.003

文献信息

• Methods for conducting assays for enzyme activity on protein microarrays
  申请人：Zhou X. Fang

  公开号：US20050118665A1

  公开（公告）日：2005-06-02

  The present invention relates to methods of conducting assays for enzymatic activity on microarrays useful for the large-scale study of protein function, screening assays, and high-throughput analysis of enzymatic reactions. The invention relates to methods of using protein chips to assay the presence, amount, activity and/or function of enzymes present in a protein sample on a protein chip. In particular, the methods of the invention relate to conducting enzymatic assays using a microarray wherein a protein and a substance are immobilized on the surface of a solid support and wherein the protein and the substance are in proximity to each other sufficient for the occurrence of an enzymatic reaction between the substance and the protein. The invention also relates to microarrays that have an enzyme and a substrate immobilized on their surface wherein the enzyme and the substrate are in proximity to each other sufficient for the occurrence of an enzymatic reaction between the enzyme and the substrate.

  本发明涉及在微阵列上进行酶活性测定的方法，这种方法可用于蛋白质功能的大规模研究、筛选测定和酶反应的高通量分析。本发明涉及使用蛋白质芯片检测蛋白质芯片上蛋白质样品中酶的存在、数量、活性和/或功能的方法。特别是，本发明的方法涉及使用芯片进行酶测定，其中蛋白质和物质被固定在固体支持物表面，蛋白质和物质相互靠近，足以使物质和蛋白质之间发生酶反应。本发明还涉及在其表面固定有酶和底物的微阵列，其中酶和底物相互靠近，足以使酶和底物之间发生酶反应。
• Cineole biodegradation: Molecular cloning, expression and characterisation of (1R)-6β-hydroxycineole dehydrogenase from Citrobacter braakii
  作者：Kate E. Slessor、Jeanette E. Stok、Sonia M. Cavaignac、David B. Hawkes、Younes Ghasemi、James J. De Voss

  DOI：10.1016/j.bioorg.2009.12.003

  日期：2010.4

  The first steps in the biodegradation of 1,8-cineole involve the introduction of an alcohol and its subsequent oxidation to a ketone. In Citrobacter braakii, cytochrome P450(cin) has previously been demonstrated to perform the first oxidation to produce (1R)-6 beta-hydroxycineole. In this study, we have cloned cinD from C. braakii and expressed the gene product, which displays significant homology to a number of short-chain alcohol dehydrogenases. It was demonstrated that the gene product of cinD exhibits (1R)-6 beta-hydroxycineole dehydrogenase activity, the second step in the degradation of 1,8-cineole. All four isomers of 6-hydroxycineole were examined but only (1R)-6 beta-hydroxycineole was converted to (1R)-6-ketocineole. The (1R)-6 beta-hydroxycineole dehydrogenase exhibited a strict requirement for NAD(H), with no reaction observed in the presence of NADP(H). The enzyme also catalyses the reverse reaction, reducing (1R)-6-ketocineole to (1R)-6 beta-hydroxycineole. During this study the N-terminal His-tag used to assist protein purification was found to interfere with NAD(H) binding and lower enzyme activity. This could be recovered by the addition of Ni2+ ions or proteolytic removal of the His-tag. (C) 2009 Elsevier Inc. All rights reserved.
• SCHENONE, SILVIA;RANISE, ANGELO;BRUNO, OLGA;BONDAVALLI, FRANCESCO, CHIM. E IND., 72,(1990) N1, C. 966
  作者：SCHENONE, SILVIA、RANISE, ANGELO、BRUNO, OLGA、BONDAVALLI, FRANCESCO

  DOI：——

  日期：——
• US7635572B2
  申请人：——

  公开号：US7635572B2

  公开（公告）日：2009-12-22
• Synthesis of oxygenated cineole derivatives from cineole: utility of cytochrome P450cin as an enantioselective catalyst
  作者：Anthony J. Farlow、Paul V. Bernhardt、James J. De Voss

  DOI：10.1016/j.tetasy.2013.02.004

  日期：2013.3

  The oxidation of cineole to (1R)-6 beta-hydroxycineole by cytochrome P450(cin) (CYP176A) is utilised as the initial step in the synthesis of a range of compounds, both novel and ones previously known only as race-mates. The potential of P450(cin) to provide useful, enantiopure building blocks is thus demonstrated. In particular, hydroxylation by this enzyme was used as the initial step in the synthesis of a range of functionalised cineole derivatives that could be used as mechanistic probes to elucidate the effect of substrate structure on the transformations mediated by P450(cin). (C) 2013 Elsevier Ltd. All rights reserved.