A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases.
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Directed evolution of Bacillus subtilis lipase A by use of enantiomeric phosphonate inhibitors: crystal structures and phage display selection.How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.Rhodococcus sp. strain CR-53 LipR, the first member of a new bacterial lipase family (family X) displaying an unusual Y-type oxyanion hole, similar to the Candida antarctica lipase clan.Computational tools for rational protein engineering of aldolases.Protein engineering of α/β-hydrolase fold enzymes.Biocatalytic synthesis of optically active tertiary alcohols.Lipase improvement: goals and strategies.Pseudomonas putida esterase contains a GGG(A)X-motif confering activity for the kinetic resolution of tertiary alcohols.Learning from directed evolution: theoretical investigations into cooperative mutations in lipase enantioselectivity.Enantiocomplementary enzymatic resolution of the chiral auxiliary: cis,cis-6-(2,2-dimethylpropanamido)spiro[4.4]nonan-1-ol and the molecular basis for the high enantioselectivity of subtilisin Carlsberg.Special Rhodococcus sp. CR-53 esterase Est4 contains a GGG(A)X-oxyanion hole conferring activity for the kinetic resolution of tertiary alcohols.Improving enantioselectivity towards tertiary alcohols using mutants of Bacillus sp. BP-7 esterase EstBP7 holding a rare GGG(X)-oxyanion hole.Activity-Fed Translation (AFT) Assay: A New High-Throughput Screening Strategy for Enzymes in Droplets.Protein Engineering and Homologous Expression of Serratia marcescens Lipase for Efficient Synthesis of a Pharmaceutically Relevant Chiral Epoxyester.Highly enantioselective kinetic resolution of two tertiary alcohols using mutants of an esterase from Bacillus subtilis.Controlling enantioselectivity of esterase in asymmetric hydrolysis of aryl prochiral diesters by introducing aromatic interactions.Double substituted variant of Bacillus amyloliquefaciens esterase with enhanced enantioselectivity and high activity towards 1-(3',4'-methylenedioxyphenyl)ethyl acetate.Discovery and Protein Engineering of Biocatalysts for Organic SynthesisAn Enzymatic Toolbox for the Kinetic Resolution of 2-(Pyridin-x-yl)but-3-yn-2-ols and Tertiary CyanohydrinsThe role of the GGGX motif in determining the activity and enantioselectivity of pig liver esterase towards tertiary alcohols
P2860
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P2860
A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases.
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年學術文章
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name
A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases.
@en
A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases.
@nl
type
label
A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases.
@en
A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases.
@nl
prefLabel
A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases.
@en
A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases.
@nl
P2860
P356
P1433
P1476
A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases.
@en
P2093
Jürgen Pleiss
Rolf D Schmid
P2860
P304
P356
10.1002/CBIC.200200518
P577
2003-06-01T00:00:00Z