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A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa

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This article is published in Journal of Organic Chemistry.The article was published on 1991-04-01. It has received 870 citations till now. The article focuses on the topics: Lipase & Candida rugosa.

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Kinetic resolution of (±)-5-bromo-12-oxa-pentacyclo-[6.2.1.16,9.02,7.02,10]dodeca-4-ene-3-endo-ol and (±)-5-bromo-13-oxa-pentacyclo[6.2.2.16,9.02,7.02,10]trideca-4-ene-3-endo-ol via Pseudomonas-mediated lipase-catalyzed transesterification

TL;DR: In this paper, the authors used three different types of lipases, including PS-C-Amano-I, to detect the transesterification of racemic alcohol to the acetate (−)-3 with 42% yield.
Journal ArticleDOI

Kinetic resolution of leishmanicidal meta and para (±)-2-[Hydroxy(nitrophenyl)methyl]acrylonitrile catalyzed by CALB: In vitro evaluations of separated meta (R), (S) and (R/S) adducts

TL;DR: In this article, the acyl derivatives enantiomers of the Morita-Baylis-Hillman adduct (±)-2-[m-nitrophenyl)methyl]acrylonitrile (1) were efficiently separated by kinetic resolution catalyzed by lipase B from Candida antarctica giving(R)-1 and (R)-2 in very high enantioselectivity (>99% e.e.).
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Cloning, expression and characterization of a new 2-Cl-propionic acid ester hydrolase from B. subtilis

TL;DR: This enzyme may serve as a model protein to solve the structure of this type of hydrolytic enzymes, which is commonly found in gene clusters of non-ribosomal peptide synthetases.
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Lipase-catalyzed asymmetric acylation of boron cluster-containing secondary alcohols

TL;DR: Utilizing lipase TL, the resolution of carborane-containing alcohol 5 is succeeded in the resolution, synthesized as a progesterone receptor ligand candidate, and the activities of the two enantiomers are evaluated.
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Novel chemoenzymatic strategy for the synthesis of enantiomerically pure secondary alcohols with sterically similar substituents.

TL;DR: A novel chemoenzymatic strategy for the synthesis of enantiomerically pure secondary alcohols with sterically similar substituents is described, and the key step is the kinetic lipase-catalyzed resolution of racemic mixtures of substituted propargylic alcohols.
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