(+/-)-1-ethylbutyl propanoate

• 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
• 英文名称: (+/-)-1-ethylbutyl propanoate
• 英文别名: 1-ethylbutyl propanoate；3-hexyl propionate；hexan-3-yl propanoate
• 化学式: C₉H₁₈O₂
• 分子量: 158.241
• InChiKey: GYZCKXAOGZSSCT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.8
• 重原子数：
  11
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.89
• 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：

  2-戊醇 、 (+/-)-1-ethylbutyl propanoate 在 Novozym 435 作用下， 生成 2-丙酸戊醇酯
  参考文献：
  名称：

  Enhancing the enantioselectivity of CALB by substrate imprinting: A combined experimental and molecular dynamics simulation model study

  摘要：

  Kinetic resolution of pentan-2-ol by CALB catalyzed enantioselective transesterification, with various alkylpropanoate acyl donors, was studied in a solid-gas reactor. Results show that the leaving alkoxy group influences the enantiomeric ratio of the reaction. Resolution of pentan-2-ol with methyl propanoate gives an enantiomeric ratio of 62. Esters with longer linear alkyl chains, from ethyl to pentyl propanoate give higher enantiomeric ratios, comprised between 103 and 117. Enantiopure ester (R)-1-methylpentyl propanoate increases the enantiomeric ratio to 140 compared with E = 120 for the racemic mixture. In contrast, enantiopure (S)-1-methylpentyl propanoate decreases the enantiomeric ratio to 72. Our data support the notion of an imprinting effect or "ligand-induced enzyme memory" caused by the shape of the leaving alcohol. To simulate the imprinting effect caused by the alkoxy part of the acyl donor, molecular modeling studies were performed with both (R)- and (S)-enantiopure 1-methylpentyl propanoate.To investigate how the first step of the reaction, through the first tetrahedral intermediate, affects the enzyme conformation depending on the enantiopure ester substrate used, 20 ns molecular dynamics simulations were carried out. Clustering analysis was done to study relevant conformations of the systems. Differences in the global conformation of the enzyme between systems with R or S enantiomers were not observed. Interestingly however, orientation of the partially buried side chain for IIe285 was affected. This could explain the increased enantiomeric ratio observed with the substrate ester (R)-1-methylpentyl propanoate due to an improved (R)-pentan-2-ol/enzyme interaction. (C) 2012 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2012.04.017
• 作为产物：
  描述：

  3-己醇 、 丙酸酐 在 4-二甲氨基吡啶 作用下， 以 二氯甲烷 为溶剂， 反应 0.17h， 以73%的产率得到(+/-)-1-ethylbutyl propanoate
  参考文献：
  名称：

  Enzymatic kinetic resolution of aliphatic sec -alcohols by LipG9, a metagenomic lipase

  摘要：

  Bioprospection for new enantioselective enzymes for application in organic synthesis is a prominent area of investigation in biocatalysis. In this context, here we present the evaluation of an immobilized lipase isolated from a metagenomic library (LipG9) for the enzymatic kinetic resolution (EKR) of aliphatic sec -alcohols, which are still challenging substrates, since low enantioselectivity values are usually observed for these resolutions. LipG9 was successfully employed in EKR of aliphatic alcohols, which were resolved with satisfactory conversions (19-59%) and enantiomeric excesses for alcohols (26-88%) and esters (30-96%) by transesterification reactions, demonstrating that its performance is equal to or better than commercially available enzymes for the same reaction. (C) 2016 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2015.12.010

文献信息

• Mutations in the stereospecificity pocket and at the entrance of the active site of Candida antarctica lipase B enhancing enzyme enantioselectivity
  作者：Z. Marton、V. Léonard-Nevers、P.-O. Syrén、C. Bauer、S. Lamare、K. Hult、V. Tranc、M. Graber

  DOI：10.1016/j.molcatb.2010.01.007

  日期：2010.8

  Two different parts of Candida antarctica lipase B (stereospecificity pocket at the bottom of the active site and hydrophobic tunnel leading to the active site) were redesigned by single- or double-point mutations, in order to better control and improve enzyme enantioselectivity toward secondary alcohols. Single-point isosteric mutations of Ser47 and Thr42 situated in the stereospecificity pocket gave rise to variants with doubled enantioselectivity toward pentan-2-ol, in solid/gas reactor. Besides, the width and shape of the hydrophobic tunnel leading to the active site was modified by producing the following single-point mutants: Ile189Ala, Leu278Val and Ala282Leu. For each of these variants a significant modification of enantioselectivity was observed compared to wild-type enzyme, indicating that discrimination of the enantiomers by the enzyme could also arise from their different accessibilities from the enzyme surface to the catalytic site. (C) 2010 Elsevier B.V. All rights reserved.
• PICOLINAMIDE COMPOUNDS WITH FUNGICIDAL ACTIVITY
  申请人：Dow Agrosciences LLC

  公开号：EP3240419B1

  公开（公告）日：2020-05-06
• Perfumes for Linear Citrus Release in Rinse-Off Systems
  申请人：Fadel Addi

  公开号：US20100087351A1

  公开（公告）日：2010-04-08

  Perfume compositions and method of formulating perfume composition are designed for use in wash-off system with a linear citrus perfume release and either any of the following effects: a desired initial release with minimal residual perfume on the targeted system, a long sustained release of fragrance, or a residual deposition of fragrance after use.
• Enzymatic kinetic resolution of aliphatic sec -alcohols by LipG9, a metagenomic lipase
  作者：Pamela T. Bandeira、Robson C. Alnoch、Alfredo R.M. de Oliveira、Emanuel M. de Souza、Fábio de O. Pedrosa、Nadia Krieger、Leandro Piovan

  DOI：10.1016/j.molcatb.2015.12.010

  日期：2016.3

  Bioprospection for new enantioselective enzymes for application in organic synthesis is a prominent area of investigation in biocatalysis. In this context, here we present the evaluation of an immobilized lipase isolated from a metagenomic library (LipG9) for the enzymatic kinetic resolution (EKR) of aliphatic sec -alcohols, which are still challenging substrates, since low enantioselectivity values are usually observed for these resolutions. LipG9 was successfully employed in EKR of aliphatic alcohols, which were resolved with satisfactory conversions (19-59%) and enantiomeric excesses for alcohols (26-88%) and esters (30-96%) by transesterification reactions, demonstrating that its performance is equal to or better than commercially available enzymes for the same reaction. (C) 2016 Elsevier B.V. All rights reserved.
• Enhancing the enantioselectivity of CALB by substrate imprinting: A combined experimental and molecular dynamics simulation model study
  作者：L. Chaput、Z. Marton、P. Pineau、L. Domon、V. Tran、M. Graber

  DOI：10.1016/j.molcatb.2012.04.017

  日期：2012.12

  Kinetic resolution of pentan-2-ol by CALB catalyzed enantioselective transesterification, with various alkylpropanoate acyl donors, was studied in a solid-gas reactor. Results show that the leaving alkoxy group influences the enantiomeric ratio of the reaction. Resolution of pentan-2-ol with methyl propanoate gives an enantiomeric ratio of 62. Esters with longer linear alkyl chains, from ethyl to pentyl propanoate give higher enantiomeric ratios, comprised between 103 and 117. Enantiopure ester (R)-1-methylpentyl propanoate increases the enantiomeric ratio to 140 compared with E = 120 for the racemic mixture. In contrast, enantiopure (S)-1-methylpentyl propanoate decreases the enantiomeric ratio to 72. Our data support the notion of an imprinting effect or "ligand-induced enzyme memory" caused by the shape of the leaving alcohol. To simulate the imprinting effect caused by the alkoxy part of the acyl donor, molecular modeling studies were performed with both (R)- and (S)-enantiopure 1-methylpentyl propanoate.To investigate how the first step of the reaction, through the first tetrahedral intermediate, affects the enzyme conformation depending on the enantiopure ester substrate used, 20 ns molecular dynamics simulations were carried out. Clustering analysis was done to study relevant conformations of the systems. Differences in the global conformation of the enzyme between systems with R or S enantiomers were not observed. Interestingly however, orientation of the partially buried side chain for IIe285 was affected. This could explain the increased enantiomeric ratio observed with the substrate ester (R)-1-methylpentyl propanoate due to an improved (R)-pentan-2-ol/enzyme interaction. (C) 2012 Elsevier B.V. All rights reserved.