(S)-quinuclidin-3-yl butyrate

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 奎宁环
• 英文名称: (S)-quinuclidin-3-yl butyrate
• 英文别名: quinuclidin-3-yl butyrate；butyric acid ester of 3-quinuclidinol；[(3S)-1-azabicyclo[2.2.2]octan-3-yl] butanoate
• 化学式: C₁₁H₁₉NO₂
• 分子量: 197.277
• InChiKey: BJNCVECKNVBHBP-SNVBAGLBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.6
• 重原子数：
  14
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.91
• 拓扑面积：
  29.5
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  溴甲苯 、 (S)-quinuclidin-3-yl butyrate 以 乙醚 为溶剂， 生成 3-butyryloxy-1-benzylquinuclidinium bromide
  参考文献：
  名称：

  Influence of the Acyl Moiety on the Hydrolysis of Quinuclidinium Esters Catalyzed by Butyrylcholinesterase

  摘要：

  Eight chiral esters of quinuclidin-3-ol and butyric, acetic, pivalic and benzoic acid were synthesized as well as their racemic and chiral, quaternary N-benzyl derivatives. All racemic and chiral quaternary compounds were studied as substrates and/or inhibitors of horse serum butyrylcholinesterase (BChE). The best substrate for the enzyme was (R)-N-benzyl butyrate. The rates of hydrolysis decreased in order (R)-butyrate >> (R)-acetate (7-fold slower) > (R)-pivalate (8-fold slower) > (R)-benzoate (9-fold slower reaction), while (S)-N-benzyl esters were much poorer substrates (320 (butyrate) - 4360-fold slower (pivalate) than the appropriate (R)-enantiomer). For all (S)-N-benzyl esters excluding (S)-N-benzyl acetate inhibition constants were determined (K-a = 3.3-60 mu mol dm(-3)). The hydrolysis of racemic mixtures of N-benzyl esters proceeded 1.4 (for acetate) - 5.1 (for benzoate) times slower than that of pure (R)-enantiomers of the corresponding concentrations due to the inhibition with (S)-enantiomers. Change of the acyl moiety of the substrate effected both activity and stereoselectivity of the BChE.(doi: 10.5562/cca1829)

  DOI：

  10.5562/cca1829
• 作为产物：
  描述：

  3-Butyryloxy-chinuclidin 在 Aspergillus melleus protease 作用下， 以 phosphate buffer 为溶剂， 反应 16.0h， 生成 (S)-(+)-3-喹宁醇 、 (R)-(-)-3-奎宁醇 、 (S)-quinuclidin-3-yl butyrate 、 (R)-quinuclidin-3-yl butyrate
  参考文献：
  名称：

  A practical chemoenzymatic process to access (R)-quinuclidin-3-ol on scale

  摘要：

  (+/-)-3-丁酰氧基奎宁环季铵盐丁酸盐6（2M，571g/L）由(+/-)-奎宁环-3-醇1和丁酸酐制得，经 fullNameAspergillus melleus fullName酶（1.0% w/v）在水溶液中进行不对称水解，同时加入Ca(OH)₂以维持反应pH7并固定由(+/-)-6引入且被酶解产生的丁酸。反应24小时后，用正庚烷萃取出(R)-奎宁环-3-基丁酸酯5a，其在甲醇中经Na₂CO₃甲氧基化后转化为(R)-1，这是作用于毒覃碱受体的神经调节剂的共同药效团，其对映体纯度为96%，总产率为从(+/-)-1的42%。不受欢迎的对映体(S)-1可通过正丁醇萃取并经其盐酸盐纯化，对映体纯度为89%，总产率为从(+/-)-1的40%。该对映体可通过Raney Co催化在含H气氛（5kg/cm²，140°C）下消旋化，以97%的产率再生(+/-)-1。(C)2003 Elsevier Science Ltd.版权归作者所有。

  DOI：

  10.1016/s0957-4166(03)00363-x

文献信息

• Process for Production of Optically Active Quinuclidinols
  申请人：Noyori Ryoji

  公开号：US20090216019A1

  公开（公告）日：2009-08-27

  A novel ruthenium complex which is a highly efficient catalyst useful for the production of optically active 3-quinuclidinols, and a process for production of optically active 3-quinuclidinols using the ruthenium complex as a catalyst, where the optically active 3-quinuclidinols are useful as an optically active, physiologically active compound utilized in medicines and agrichemicals or as a synthetic intermediate such as a liquid crystal material.

  一种新颖的钌配合物，是一种高效催化剂，可用于生产光学活性的3-喹诺啉醇，并且提供一种以该钌配合物为催化剂生产光学活性3-喹诺啉醇的方法，其中光学活性的3-喹诺啉醇可用作光学活性、生理活性的化合物，用于药物和农药，或者作为合成中间体，如液晶材料。
• [EN] PROCESS FOR PRODUCING OPTICALLY ACTIVE ALCOHOL IN THE PRESENCE OF RHODIUM, A CHIRAL FERROCENYLDIPHOSPHINE AND AN OPTICALLY ACTIVE DIAMINE<br/>[FR] PROCEDE DE PRODUCTION D'UN ALCOOL OPTIQUEMENT ACTIF EN PRESENCE DE RHODIUM, FERROCENYLDIPHOSPHINE CHIRALE ET DIAMINE OPTIQUEMENT ACTIVE
  申请人：KAWAKEN FINE CHEMICALS CO

  公开号：WO2004078686A1

  公开（公告）日：2004-09-16

  A novel process for producing optically active alcohols through asymmetric hydrogenation of prochiral carbonyl compounds allows high-yield, industrially favorable production of an optically active alcohol at a high enantiomeric excess. The process is charaterized in that the asymmetric hydrogenation is carried out in the absence of a base and in the presence of a rhodium complex or a salt thereof; an optically active ferrocenyl diphosphine; and an optically active diamine.

  通过对具有手性氢化合物的不对称氢化，可以通过一种新型工艺生产光学活性醇，实现高产率、工业上有利的光学活性醇生产，其旋光异构体过量高。该工艺的特点是，在无碱存在的情况下，采用铑配合物或其盐；光学活性二膦基二茂铁；以及光学活性二胺进行不对称氢化。
• Methods for producing optically active alcohols
  申请人：Daicel Chemical Industries, Ltd.

  公开号：EP1318200A2

  公开（公告）日：2003-06-11

  A method for producing optically active alcohols is provided. Optically active alcohols are useful intermediates in pharmaceutical production. The method of the present invention enables simple and efficient production of optically active alcohols with a high optical purity. According to the production method disclosed, optically active alcohols are produced via asymmetric reduction of 3-quinuclidinone using tropinone reductase-I. For example, the use of tropinone reductase-I derived from plants like Datura stramonium and Hyoscyamus niger allows the production of high optical purity (R)-3-quinuclidinol as shown in Formula (1) below.

  提供了一种生产光学活性醇的方法。光学活性醇是药品生产中有用的中间体。本发明的方法可以简单高效地生产出光学纯度高的光学活性醇。根据所公开的生产方法，光学活性醇是通过使用托品酮还原酶-I不对称还原 3-奎宁环酮生产的。例如，使用从曼陀罗（Datura stramonium）和黑升麻（Hyoscyamus niger）等植物中提取的托品酮还原酶-I，可以生产出光学纯度很高的（R）-3-奎宁环醇，如下式（1）所示。
• PROCESS FOR PRODUCTION OF OPTICALLY ACTIVE QUINUCLIDINOL
  申请人：Nagoya Industrial Science Research Institute

  公开号：EP1867654B1

  公开（公告）日：2014-06-11
• Simple one-pot process for the bioresolution of tertiary amino ester protic ionic liquids using subtilisin
  作者：Maude Brossat、Thomas S. Moody、Stephen J.C. Taylor、Jonathan W. Wiffen

  DOI：10.1016/j.tetasy.2009.09.007

  日期：2009.9

  An efficient hydrolase-catalyzed bioresolution of tertiary amino ester protic ionic liquids has been demonstrated. Protic ionic liquids have been prepared in one step from the corresponding tertiary amino alcohols by treatment with butyric anhydride. After bioresolution, unreacted esters can be easily separated from the corresponding alcohols by extraction with hexane Bioresolution of quinuclidin-3-yl butyrate has been performed with excellent selectivity. (C) 2009 Elsevier Ltd. All rights reserved.