(R)-5-methylhex-1-en-3-ol

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (R)-5-methylhex-1-en-3-ol
• 英文别名: (3R)-5-methylhex-1-en-3-ol
• 化学式: C₇H₁₄O
• 分子量: 114.188
• InChiKey: AZAKXXGZWJWZLN-ZETCQYMHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  8
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  20.2
• 氢给体数：
  1
• 氢受体数：
  1

反应信息

• 作为产物：
  描述：

  异戊醛 在 Candida antarctica lipase B 作用下， 以 四氢呋喃 、 乙醚 、 正己烷 为溶剂， 反应 12.5h， 生成 (R)-5-methylhex-1-en-3-ol 、 (S)-5-methylhex-1-en-3-yl acetate
  参考文献：
  名称：

  Highly Efficient Kinetic Resolution of Allylic Alcohols with Terminal Double Bond

  摘要：

  在本研究中，采用脂肪酶催化的动力学解析（Novozyme 435）制备了端双键的手性烯丙醇和醋酸酯，恩基异纯度范围为94%至99%。

  DOI：

  10.2174/157017811799304151

文献信息

• Kinetic resolution of racemic secondary aliphatic allylic alcohols in lipase-catalyzed transesterification
  作者：Anna Chojnacka、Robert Obara、Czesław Wawrzeńczyk

  DOI：10.1016/j.tetasy.2006.12.020

  日期：2007.1

  Different lipases were screened as biocatalysts in the kinetic resolution process of (+/-)-hept-1-en-3-ol 1, (+/-)-5-methylhex-1-en3-ol 2, (+/-)-6-methythept-2-en-4-ol 3, (+/-)-6,6-dimethylhept-2-en-4-ol 4, and 1-phenylbut-3-en-2-ol 5 by enantio selective transesterification. The acylation of (+/-)-l and (+/-)-2 catalyzed by Novozym 435 (Candida antarctica) was very effective and proceeded with good enantioselectivity. After 4-8 h of reactions the esters formed and the alcohols, which remained were obtained with high enantiomeric excess with 97-100% ee and 91-100% ee, respectively. The lipase Amano PS (Burkholderia cepacia) was the best catalyst in the asymmetric transesterification of (+/-)-5 affording the (R)-alcohol with 90-95% ee and the (S)-ester with 98-100% ce. Low enantio selectivities were observed in the cases of lipase-catalyzed acylation of (+/-)-3 and (+/-)-4. (c) 2007 Elsevier Ltd. All rights reserved.
• Highly Efficient Kinetic Resolution of Allylic Alcohols with Terminal Double Bond
  作者：Francisco A. Marques、Marcos A. Oliveira、Gustavo Frensch、Beatriz Helena L. N. Sales Maia、Andersson Barison、Cesar A. Lenz、Palimecio G. Guerrero

  DOI：10.2174/157017811799304151

  日期：2011.12.1

  In this study, the lipase-catalyzed kinetic resolution (Novozyme 435) was employed to prepare chiral allylic alcohols and acetates with terminal double bonds in enantiomeric excesses ranging from 94 to 99 %.

  在本研究中，采用脂肪酶催化的动力学解析（Novozyme 435）制备了端双键的手性烯丙醇和醋酸酯，恩基异纯度范围为94%至99%。