(Q57189496)

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Site directed mutagenesis of recombinant pig liver esterase yields mutants with altered enantioselectivity

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Site directed mutagenesis of recombinant pig liver esterase yields mutants with altered enantioselectivity (English)

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Anna Musidlowska-Persson

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1

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Uwe T. Bornscheuer

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2

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publication date

May 2003

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published in

Tetrahedron: Asymmetry

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volume

14

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issue

10

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page(s)

1341-1344

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cites work

Characterization of the Isoenzymes of Pig-Liver Esterase 1. Chemical Studies. 1. Chemical Studies

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https://api.crossref.org/works/10.1016%2FS0957-4166%2803%2900205-2

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7 January 2021

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Characterization of the Isoenzymes of Pig-Liver Esterase 2. Kinetic Studies. 2. Kinetic Studies

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https://api.crossref.org/works/10.1016%2FS0957-4166%2803%2900205-2

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7 January 2021

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By Overexpression in the YeastPichia pastoris to Enhanced Enantioselectivity: New Aspects in the Application of Pig Liver Esterase

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https://api.crossref.org/works/10.1016%2FS0957-4166%2803%2900205-2

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7 January 2021

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Substrate specificity of the γ-isoenzyme of recombinant pig liver esterase towards acetates of secondary alcohols

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https://api.crossref.org/works/10.1016%2FS0957-4166%2803%2900205-2

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7 January 2021

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Purification and molecular cloning of porcine intestinal glycerol-ester hydrolase--evidence for its identity with carboxylesterase

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7 January 2021

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10.1016/S0957-4166(03)00205-2

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(Q57189496)

Site directed mutagenesis of recombinant pig liver esterase yields mutants with altered enantioselectivity

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