valeric acid (d)-menthyl ester | 186095-05-6

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: valeric acid (d)-menthyl ester
• 英文别名: [(1S,2R,5S)-5-methyl-2-propan-2-ylcyclohexyl] pentanoate
• CAS: 186095-05-6
• 化学式: C₁₅H₂₈O₂
• 分子量: 240.386
• InChiKey: LCJPVSLESAPYMK-MJBXVCDLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5
• 重原子数：
  17
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.93
• 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：

  1-碘己烷 、 valeric acid (d)-menthyl ester 在 六甲基磷酰三胺 、 lithium diisopropyl amide 作用下， 生成
  参考文献：
  名称：

  Alkylation ofl- andd-Menthyl Pentanoate with (20S)-20-Iodomethyl-4α-methyl-5α-pregnane

  摘要：

  The alkylation of l- and d-menthyl valerate with n-hexyl iodide and with (20S)-20-iodomethyl-4 alpha-methyl-5 alpha-pregnane gave modest levels of diastereoselection. The chirality of the ester group favoured slight degree of selectivity. The chiral centers had limited impact on diastereoselectivity.

  DOI：

  10.1080/00397919608004775
• 作为产物：
  描述：

  D-薄荷醇 、 正戊酸 以 甲苯 为溶剂， 生成 valeric acid (d)-menthyl ester
  参考文献：
  名称：

  Candida rugosa lipase: Enantioselectivity enhancements in organic solvents

  摘要：

  Chiral resolutions of carboxylic acids (1-3) and alcohol (4) were carried out through esterification or transesterification in organic solvents using cross-linked enzyme crystals (CLEC(R)) of Candida rugosa lipase (CRL). Comparison of these results with those of elude CRL reveal significant differences. As was seen in resolution through hydrolysis,(1) a marked improvement in enantioselectivity is realized with the CLEC. Additionally, the stability afforded the enzyme in CLEC form leads to a higher activity in organic solvent. Copyright (C) 1996 Elsevier Science Ltd

  DOI：

  10.1016/0040-4039(96)01430-x

文献信息

• METHOD OF SYNTHESIZING BEPOTASTINE OR BENZENESULFONIC ACID SALT THEREOF AND INTERMEDIATES USED THEREIN
  申请人：EVERLIGHT USA, INC.

  公开号：US20140046068A1

  公开（公告）日：2014-02-13

  The present invention relates to a novel method of synthesizing bepotastine or its benzenesulfonic acid salt and novel intermediates used therein. The present invention uses L-α-hydroxy acid for chiral resolution to form an L-α-hydroxy acid salt of a compound represented by the following formula (VII-1), so as to synthesize bepotastine or its benzenesulfonic acid salt in high optical purity.

  本发明涉及一种合成贝泼替丁或其苯磺酸盐的新方法以及其中使用的新中间体。本发明利用L-α-羟基酸进行手性分离，形成由以下式（VII-1）所代表的化合物的L-α-羟基酸盐，从而在高光学纯度下合成贝泼替丁或其苯磺酸盐。
• A Structural Basis for the Chiral Preferences of Lipases
  作者：Miroslaw Cygler、Pawel Grochulski、Romas J. Kazlauskas、Joseph D. Schrag、Francois Bouthillier、Byron Rubin、Alessio N. Serreqi、Ajay K. Gupta

  DOI：10.1021/ja00087a002

  日期：1994.4

  Many lipases and esterases show striking similarities in their enantioselectivities, and empirical rules have been formulated to predict the preferred stereochemistry for various types of reactions. A rule for formation of secondary alcohols predicts which enantiomer reacts faster based on the relative sizes of the substituents at the stereocenter. We report the first direct determination of the mechanism by which a lipase distinguishes between enantiomers and provide a general structural explanation of the aforementioned empirical rule. We determined X-ray crystal structures of covalent complexes of Candida rugosa lipase with transition-state analogs for the hydrolysis of menthyl esters. One structure contains (1R)-menthyl hexylphosphonate, 1R, derived from the fast-reacting enantiomer of menthol; the other contains (1S)-menthyl hexylphosphonate, 1S, derived from the slow-reacting enantiomer. These high-resolution three-dimensional structures show, firstly, that the empirical rule determined by substrate mapping is a good low-resolution description of the alcohol binding site in Candida rugosa lipase. Secondly, interactions between the menthyl ring of the slow-reacting enantiomer and the histidine of the catalytic triad disrupt the hydrogen bond between N epsilon 2 of the imidazole ring and the menthol oxygen atom, likely accounting for the slower reaction of the (1S)-enantiomer of menthol. Thirdly, the enantiopreference of CRL toward secondary alcohols is set, not by an alcohol binding site separate from the catalytic site but by the same loops that assemble the catalytic machinery. The common orientation of these loops among many lipases and esterases accounts for their common enantiopreference toward secondary alcohols. This identification of the enantioselection mechanism sets the stage for rational enantioselective syntheses with lipases.