(R)-5-hydroxyoctan-4-one

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (R)-5-hydroxyoctan-4-one
• 英文别名: (R)-Butyroin；(5R)-5-hydroxyoctan-4-one
• 化学式: C₈H₁₆O₂
• 分子量: 144.214
• InChiKey: BVEYJWQCMOVMAR-SSDOTTSWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  10
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  37.3
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  5-羟基-4-辛酮 在 乙酸乙烯酯 、 Lipase Amano PS 作用下， 以 正己烷 为溶剂， 反应 24.0h， 以32%的产率得到(R)-5-hydroxyoctan-4-one
  参考文献：
  名称：

  Biocatalytic racemization of synthetically important functionalized α-hydroxyketones using microbial cells

  摘要：

  Biocatalytic racemization of straight-chain and cyclic acyloins bearing (halo)alkyl, alkenyl and functionalized (hetero)aryl moieties was accomplished using whole resting cells of bacteria, fungi and yeasts. Mild physiological reaction conditions ensured the suppression of undesired side-reactions, such as elimination or condensation. This biocatalytic protocol represents a useful tool for the clean racemization of unwanted enantiomers of synthetically important alpha-hydroxyketones derived from kinetic resolution. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetasy.2007.06.005

文献信息

• Asymmetric Ozone Oxidation of Silylalkenes Using a<i>C</i>₂-Symmetrical Dialkoxysilyl Group as a Chiral Auxiliary
  作者：Kazunobu Igawa、Yuuya Kawasaki、Kosuke Nishino、Naoto Mitsuda、Katsuhiko Tomooka

  DOI：10.1002/chem.201402996

  日期：2014.7.21

  Ozone oxidation of silyl‐substituted alkenes, namely silylalkenes, proceeds in an addition‐type manner to afford α‐silylperoxy carbonyl compounds in good to excellent yields, without the formation of normal ozonolysis products. Herein the ozone oxidation of chiral alkenylsilanes prepared from alkynes and a newly designed chiral hydrosilane is reported. The reaction affords silylperoxides with high

  甲硅烷基取代的烯烃（即甲硅烷基烯烃）的臭氧氧化反应以加成方式进行，从而以良好的产率提供了优异的α-甲硅烷基过氧羰基化合物，而没有形成常规的臭氧分解产物。本文报道了由炔烃和新设计的手性氢硅烷制得的手性烯基硅烷的臭氧氧化。该反应提供具有高非对映选择性（高达94％dr）的甲硅烷基过氧化物。甲硅烷基过氧化物可以立体有择的方式转化为对映体富集的手性酰基辅酶。
• Enzyme-catalyzed C–C bond formation using 2-methyltetrahydrofuran (2-MTHF) as (co)solvent: efficient and bio-based alternative to DMSO and MTBE
  作者：Saravanakumar Shanmuganathan、Dessy Natalia、Anne van den Wittenboer、Christina Kohlmann、Lasse Greiner、Pablo Domínguez de María

  DOI：10.1039/c0gc00590h

  日期：——

  The enzymatic carboligation of aldehydes (C–C bond formation) catalyzed by benzaldehyde lyase (BAL) affords chiral α-hydroxy-ketones under mild reaction conditions in aqueous media. To enhance substrate and product availability under aqueous conditions, processes are often set-up using either DMSO as co-solvent, or MTBE as second organic phase. Although efficient, DMSO leads to difficulties in separation during downstream processing, with wastewater formation. MTBE provides a cleaner and straightforward work-up, but its petrochemical origin, together with its poor degradability, gives rise to environmental concerns. Herein it is reported that 2-methyltetrahydrofuran (2-MTHF) is a promising candidate to substitute DMSO or MTBE in lyase-catalyzed reactions. 2-MTHF can be derived from bio-based resources (e.g. levulinic acid), and it is abiotically degraded by air. When BAL is added to buffer-2-MTHF (5% v/v) mixtures, enzyme remains stable with a half-life of 178 ± 8 h, with productivities (benzoin synthesis) of 10 g benzoin L−1h−1. Several BAL-catalyzed aldehyde carboligations were assessed under those conditions, leading in all cases to high isolated yield (quantitative in majority), and to high enantioselectivity (up to >99%). Furthermore, preliminary results obtained with two phase systems in the BAL-catalyzed benzoin synthesis afforded 60 g benzoin L−1 in 24 h (ee > 99%). Therefore, 2-MTHF may be a valuable (co)solvent, not only to tackle environmental concerns, but also in terms of practical, efficient biocatalysis.

  在水介质中，苯甲醛裂解酶（BAL）催化的醛的酶碳化反应（CâC 键形成）可在温和的反应条件下生成手性 δ- 羟基酮。为了提高水介质条件下底物和产物的利用率，通常使用 DMSO 作为助溶剂或 MTBE 作为第二有机相进行工艺设置。DMSO 虽然高效，但在下游处理过程中难以分离，还会产生废水。MTBE 提供了一种更清洁、更直接的加工方法，但其来源于石油化工，降解性差，引起了环境问题。据报道，在裂解酶催化反应中，2-甲基四氢呋喃（2-MTHF）是替代二甲基亚砜（DMSO）或 MTBE 的理想候选物质。2-MTHF 可从生物资源（如乙酰丙酸）中提取，并可被空气非生物降解。当 BAL 添加到缓冲液-2-MTHF（5% v/v）混合物中时，酶保持稳定，半衰期为 178 ± 8 h，生产率（安息香合成）为 10 g benzoin Lâ1hâ1。在这些条件下，评估了几种 BAL 催化的醛羰基化反应，在所有情况下都有很高的分离产率（大部分为定量产率）和很高的对映选择性（高达 >99%）。此外，在 BAL 催化的安息香合成中使用两相体系所获得的初步结果显示，在 24 小时内就能得到 60 克安息香 Lâ1（ee > 99%）。因此，2-MTHF 可能是一种有价值的（辅助）溶剂，不仅能解决环境问题，还能用于实用、高效的生物催化。
• Branched-Chain Keto Acid Decarboxylase fromLactococcus lactis (KdcA), a Valuable Thiamine Diphosphate-Dependent Enzyme for Asymmetric CC Bond Formation
  作者：Dörte Gocke、Cong Luan Nguyen、Martina Pohl、Thomas Stillger、Lydia Walter、Michael Müller

  DOI：10.1002/adsc.200700057

  日期：2007.6.4

  The thiamine diphosphate-dependent, branched-chain 2-keto acid decarboxylase from Lactococcus lactis sup. cremoris B1157 (KdcA) is a new valuable enzyme for the synthesis of chiral 2-hydroxy ketones. The gene was cloned and the enzyme was expressed as an N-terminal hexahistidine fusion protein in Escherichia coli. It has a broad substrate range for the decarboxylation reaction including linear and

  源自乳酸乳球菌的硫胺素二磷酸依赖性的支链2-酮酸脱羧酶。乳脂B1157（KDCA）为手性2-羟基酮的合成一个新的有价值的酶。克隆了该基因，并将该酶表达为大肠杆菌中的N端六组氨酸融合蛋白。它具有广泛的脱羧反应底物范围，包括直链和支链脂族和芳族酮酸，以及丙酮酸苯酯和吲哚-3-丙酮酸酯。重组KdcA的二聚体结构与其他2-酮酸脱羧酶的四聚体结构相反。该酶在pH 5至7之间稳定，最适合脱羧反应的pH 6-7。尽管KdcA在高达40°C的温度下足够稳定，但它在较高温度下会迅速失去活性。在这项工作中，首次证明了KdcA的碳氧合酶活性。该酶显示出异常广泛的底物范围，最引人注目的是，它催化不同的芳族醛以及CH-酸性醛（如苯乙醛和吲哚-3-乙醛）与脂族醛（如乙醛）的羰基化反应，丙醛和环丙烷甲醛，产生高对映体过量的手性2-羟基酮。值得注意的是，供体-受体的选择性受各个底物组合的性质的强烈影响。
• Asymmetric Synthesis of Aliphatic 2-Hydroxy Ketones by Enzymatic Carboligation of Aldehydes
  作者：Pablo Domínguez de María、Martina Pohl、Dörte Gocke、Harald Gröger、Harald Trauthwein、Thomas Stillger、Lydia Walter、Michael Müller

  DOI：10.1002/ejoc.200600876

  日期：2007.6

  asymmetric ligation of aliphatic aldehydes to afford enantiomerically enriched 2-hydroxy ketones. Carboligation of linear aldehydes with both enzymes results in high levels of conversion and in enantioselectivities of up to 80 % ee. In cases involving branched aliphatic aldehydes, BAL enables the carboligation of 3-methylbutanal with a high level of conversion and an enantioselectivity of 89 % ee. ((c)

  苯甲醛裂解酶 (BAL) 和苯甲酰甲酸脱羧酶 (BFD) 催化脂肪醛的不对称连接，得到富含对映体的 2-羟基酮。线性醛与两种酶的碳化作用导致高水平的转化率和高达 80% ee 的对映选择性。在涉及支链脂肪醛的情况下，BAL 能够以高转化率和 89% ee 的对映选择性进行 3-甲基丁醛的碳化反应。((c) Wiley-VCH Verlag GmbH & Co.
• Benzaldehyde lyase (BAL)-catalyzed enantioselective CC bond formation in deep-eutectic-solvents–buffer mixtures
  作者：Zaira Maugeri、Pablo Domínguez de María

  DOI：10.1016/j.molcatb.2014.06.003

  日期：2014.9

  Deep-eutectic-solvents (DES) have emerged in the last decades as promising bio-based and biodegradable neoteric solvents for biocatalysis, with examples covering different enzymes (mostly hydrolases) and whole-cells (baker's yeast). This paper explores for the first time the use of benzaldehyde lyase (BAL), a thiamine-diphosphate dependent lyase (ThDP-lyase) able to catalyze the carboligation of aldehydes

  在过去的几十年中，深层共溶剂（DES）作为一种有前途的生物基和可生物降解的新型生物溶剂用于生物催化而出现，其实例涵盖了不同的酶（主要是水解酶）和全细胞（面包酵母）。本文首次探讨了苯甲醛合酶（BAL）的使用，该酶是一种硫胺素-二磷酸依赖型合酶（ThDP-合酶），能够催化不同DES-缓冲液混合物中醛的碳转移（CC键形成）。通过使用氯化胆碱-甘油DES，BAL在60:40 DES-缓冲液（v / v）时仍具有出色的对映选择性，从而保持了充分的活性，从而在70:30的混合物中观察到了明显的变性。值得注意的是，使用氯化胆碱-脲DES作为反应介质可在这种溶剂-缓冲剂比例下完全转化为BAL，