(1R,2R)-反式-1,2-环己二醇二乙酸酯 | 130464-07-2

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 中文名称: (1R,2R)-反式-1,2-环己二醇二乙酸酯
• 英文名称: (R,R)-1,2-diacetoxycyclohexane
• 英文别名: trans-1,2-Diacetoxy-cyclohexan；cis-1,2-Cyclohexanediol diacetate；[(1R,2R)-2-acetyloxycyclohexyl] acetate
• CAS: 130464-07-2
• 化学式: C₁₀H₁₆O₄
• 分子量: 200.235
• InChiKey: NSTPWRQTPXJRSP-NXEZZACHSA-N

物化性质

• 熔点：
  57-59 °C
• 沸点：
  249.7±33.0 °C(Predicted)
• 密度：
  1.09±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.3
• 重原子数：
  14
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.8
• 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：

  (1R,2R)-反式-1,2-环己二醇二乙酸酯 在 pseudomonas fluorescens lipase 作用下， 反应 6.0h， 以33%的产率得到trans-2-acetoxy-1-cyclohexanol
  参考文献：
  名称：

  对荧光假单胞菌脂肪酶催化的环状乙酸酯的对映选择性水解的见解

  摘要：

  用荧光假单胞菌脂肪酶（PFL）水解外消旋乙酸酯，得到具有R-构型的旋光性醇，与环的大小无关。提出了PFL催化水解的三点模型。

  DOI：

  10.1039/c39880000966
• 作为产物：
  描述：

  trans-1,2-cyclohexandiol 在 lipase AK 、 sodium carbonate 作用下， 以 乙酸乙酯 为溶剂， 反应 24.0h， 生成 (1R,2R)-反式-1,2-环己二醇二乙酸酯
  参考文献：
  名称：

  Kinetic resolution of trans-2-acetoxycycloalkan-1-ols by lipase-catalysed enantiomerically selective acylation

  摘要：

  Kinetic resolution of a series of racemic trans-cycloalkane-1.2-diol monoacetates rac-2a-d was performed by enantiomerically selective transesterification with vinyl acetate catalysed by commercial and our own-prepared fungal lipases to yield diacetates (R,R)-3a-d and monoacetates (S,S)-2a-d in high enantiomeric purity. The monoacetates (R,R)-2a-d were also prepared from the racemic diacetates rac-3a-d by lipase-catalysed hydrolysis. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(03)00568-8

文献信息

• Enzymatic preparation of optically pure trans-1,2-cycloalkanediols
  作者：R. Seemayer、M. P. Schneider

  DOI：10.1039/c39910000049

  日期：——

  trans-1,2-Cycloalkanediols (R,R)-1–4 and (S,S)-1–3 of high optical purities are prepared by enzymatic hydrolysis and esterification catalysed by a lipase from Pseudomonas sp. (SAM II).

  高光学纯度的反式-1,2-环烷二醇(R,R)-1–4和(S,S)-1–3是通过由假单胞菌(SAM II)催化的酶解和酯化反应制备的。
• Adrenaline profiling of lipases and esterases with 1,2-diol and carbohydrate acetates
  作者：Denis Wahler、Olivier Boujard、Fabrice Lefèvre、Jean-Louis Reymond

  DOI：10.1016/j.tet.2003.11.059

  日期：2004.1

  The adrenaline test for enzymes is a general back-titration procedure to detect 1,2-diols, 1,2-aminoalcohols and alpha-hydroxyketones reaction products of enzyme catalysis by colorimetry. The method was used to profile a series of esterases and lipases for their esterolytic activity on a series of carbohydrate and polyol acetates. Substrates were prepared by peracetylation and used for parallel microtiter-plate analysis of enzyme activities. This method can be used to achieve a rapid and automated characterization of a set of enzymes during HTS screening. (C) 2003 Elsevier Ltd. All rights reserved.
• Laine, Dramane; Fujita, Morifumi; Ley, Steven V., Journal of the Chemical Society. Perkin transactions I, 1999, # 12, p. 1639 - 1645
  作者：Laine, Dramane、Fujita, Morifumi、Ley, Steven V.

  DOI：——

  日期：——
• Enantioselective acylation of alcohols catalyzed by lipase QL from Alcaligenes sp.: A predictive active site model for lipase QL to identify the faster reacting enantiomer of an alcohol in this acylation
  作者：Koichiro Naemura、Masaki Murata、Rie Tanaka、Masashi Yano、Keiji Hirose、Yoshito Tobe

  DOI：10.1016/0957-4166(96)00186-3

  日期：1996.6

  Lipase QL-catalyzed acylation of secondary alcohols using isopropenyl acetate as the acylating agent in diisopropyl ether gave preferentially the corresponding acetate with an R configuration. On the basis of the results, a predictive active site model for lipase QL is proposed for identifying which enantiomer of a secondary alcohol reacts faster in this reaction. (C) 1996 Elsevier Science Ltd
• Enantioselective acylation of primary and secondary alcohols catalyzed by lipase QL from Alcaligenes sp.: A predictive active site model for lipase QL to identify which enantiomer of an alcohol reacts faster in this acylation
  作者：Koichiro Naemura、Masaki Murata、Rie Tanaka、Masashi Yano、Keiji Hirose、Yoshito Tobe

  DOI：10.1016/0957-4166(96)00429-6

  日期：1996.11

  Lipase QL (from Alcaligenes sp.)-catalyzed acylation of alcohols using isopropenyl acetate as the acylating agent in diisopropyl ether converted preferentially primary alcohols with an S configuration and secondary alcohols with an R configuration into the corresponding homochiral acetates. On the basis of observed enantiomer selectivities, a predictive active site model for lipase QL is proposed for identifying which enantiomer of a primary or a secondary alcohol reacts faster in this acylation. Copyright (C) 1996 Published by Elsevier Science Ltd

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