(R,S)-2-(pyridin-4-yl)but-3-yn-2-yl acetate | 1233717-97-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吡啶及其衍生物
• 英文名称: (R,S)-2-(pyridin-4-yl)but-3-yn-2-yl acetate
• 英文别名: 2-(4-Pyridyl)but-3-yn-2-yl acetate；2-pyridin-4-ylbut-3-yn-2-yl acetate
• CAS: 1233717-97-9
• 化学式: C₁₁H₁₁NO₂
• 分子量: 189.214
• InChiKey: WUJJJZCBXOUXAP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  14
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  39.2
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (R,S)-2-(pyridin-4-yl)but-3-yn-2-yl acetate 在 EstA₁ 作用下， 生成
  参考文献：
  名称：

  Identification of novel esterases for the synthesis of sterically demanding chiral alcohols by sequence-structure guided genome mining

  摘要：

  Six esterases isolated from sequence and structure-guided genome mining approaches were evaluated for the kinetic resolution of secondary and tertiary alcohols that find application in the fine chemical and pharmaceutical industries. Activity and enantioselectivity with E-values of up to 24 were determined towards a range of sterically demanding tertiary alcohol esters. Excellent enantioselectivity (E > 100) was also achieved in the hydrolysis of a less challenging secondary alcohol ester, menthyl acetate. These results highlight that these approaches can be used for the identification of novel esterases applicable to the preparation of commercially desirable alcohols. (C) 2011 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.molcatb.2011.02.009
• 作为产物：
  描述：

  乙酰氯 、 2-(pyridin-4-yl)but-3-yn-2-ol 在 正丁基锂 作用下， 以 四氢呋喃 、 乙醚 为溶剂， 反应 1.25h， 以47%的产率得到(R,S)-2-(pyridin-4-yl)but-3-yn-2-yl acetate
  参考文献：
  名称：

  2-(吡啶-x-基)but-3-yn-2-ols 和叔氰醇动力学拆分的酶工具箱

  摘要：

  已经通过使用在大肠杆菌中表达的几种重组羧基酯酶及其变体研究了一系列带有氮取代基的叔醇乙酸酯的动力学拆分。大多数酶在这些叔醇的转化中具有活性，并且在合成三个 2-(吡啶-x-基)but-3-yn-2-ols 时实现了优异的对映选择性，其中吡啶环中的氮原子为2'-、3'-和 4'-位置。由于酶的对映选择性通常较低，因此叔氰醇的拆分被证明更加困难。然而，获得了具有 99% ee 的 (S)-1-氰基-2,2,2-三氟-1-苯基乙酸乙酯。结果表明，在一系列叔醇的合成中，单个酶的底物范围有限，可以通过使用不同酶的组合来有效克服。© 2010 Wiley-VCH Verlag GmbH & Co. KGaA。

  DOI：

  10.1002/ejoc.201000193

文献信息

• Characterization of a novel esterase isolated from intertidal flat metagenome and its tertiary alcohols synthesis
  作者：Ki-Hoon Oh、Giang-Son Nguyen、Eun-Young Kim、Robert Kourist、Uwe Bornscheuer、Tae-Kwang Oh、Jung-Hoon Yoon

  DOI：10.1016/j.molcatb.2012.04.015

  日期：2012.8

  A gene coding for an esterase (EstEH112) was isolated from metagenome originated from Korean intertidal flat sediment. The putative esterase gene encoded a 340 amino acids protein with characteristic residues of lipolytic enzymes such as a conserved pentapeptide (GXSXG), the typical catalytic S-D-H triad, and a GGG(A)X-motif in the oxyanion hole near the active site similar to the hormone sensitive lipase (HSL) family. p-Nitrophenyl butyrate was the best substrate for the enzyme among the other p-nitrophenyl esters investigated. The apparent optimal temperature and pH for EstEH112 was 35 C and at pH 8.0, respectively. EstEH112 efficiently catalyzed the hydrolysis of various large tertiary alcohol esters. These characteristics of EstEH112 make it a potential candidate for application in biocatalysis. (C) 2012 Elsevier B.V. All rights reserved.