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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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Long-distance control in stereoselective reduction of 3-[3-(4′-bromo[1,1′-biphenyl]-4-yl)-3-keto-1-phenylpropyl]-4-hydroxy-2H-1-benzopyran-2-one: Relative configuration of prevailing diastereomer and absolute configuration of its enantiomers

TL;DR: In this paper, the diastereomeric racemates 4A and 4B are separated and their respective syn and anti configurations are assigned on the bases of mechanic considerations, supported by the 1H-NMR spectra and conformational analysis based on MM2 calculations.
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Preparation of (R)- and (S)-4-chloro-3-acetoxybutyronitrile using microbial resolution

TL;DR: A new preparation of optically active 4-chloro-3-acetoxybutyronitrile (AcBN) was developed using the resting cells of bacteria based on enantioselective hydrolysis of the ester function of the substrate.
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Site-specifically Incorporated Non-Canonical Amino Acids into Pseudomonas alcaligenes Lipase to Hydrolyze L-menthol Propionate among the Eight Isomers

TL;DR: The four ncAAs were site‐specifically incorporated into a lipase (PaL) produced by Pseudomonas alcaligenes to explore its diastereopreference mechanism and several variants with significant improvement in the diastreopreference were obtained.
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A Semiautomated Structure-Based Method To Predict Substrates of Enzymes via Molecular Docking: A Case Study with Candida antarctica Lipase B

TL;DR: An open-source, extensible, and flexible software platform for predicting enzyme substrates called THEMIS, which performs in silico virtual screening for potential catalytic targets of an enzyme on the basis of the enzyme's catalysis mechanism, and is perhaps the first reported scheme to meet the requirement for practical applicability to enzyme studies.
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Cutinases as stereoselective catalysts: Specific activity and enantioselectivity of cutinases and lipases for menthol and its analogs

TL;DR: Results of this study highlight that cutinases can provide important advantages relative to lipases for enantioselective transformation, most notably with bulky and sterically hindered substrates.
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