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Enantioselective enzymes by computational design and in silico screening
University of Groningen, The Netherlands.
University of Groningen, The Netherlands.
University of Washington, USA.ORCID iD: 0000-0002-9300-614X
University of Groningen, The Netherlands.
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2015 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 54, no 12, p. 3726-3730Article in journal (Refereed) Published
Abstract [en]

Computational enzyme design holds great promise for providing new biocatalysts for synthetic chemistry. A strategy to design small mutant libraries of complementary enantioselective epoxide hydrolase variants for the production of highly enantioenriched (S,S)-diols and (R,R)-diols is developed. Key features of this strategy (CASCO, catalytic selectivity by computational design) are the design of mutations that favor binding of the substrate in a predefined orientation, the introduction of steric hindrance to prevent unwanted substrate binding modes, and ranking of designs by high-throughput molecular dynamics simulations. Using this strategy we obtained highly stereoselective mutants of limonene epoxide hydrolase after experimental screening of only 37 variants. The results indicate that computational methods can replace a substantial amount of laboratory work when developing enantioselective enzymes.

Place, publisher, year, edition, pages
2015. Vol. 54, no 12, p. 3726-3730
National Category
Chemical Sciences Biochemistry and Molecular Biology
Research subject
Natural Science, Chemistry
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URN: urn:nbn:se:lnu:diva-50605DOI: 10.1002/anie.201411415PubMedID: 25651000OAI: oai:DiVA.org:lnu-50605DiVA, id: diva2:911188
Available from: 2016-03-11 Created: 2016-03-11 Last updated: 2019-02-26Bibliographically approved

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Bjelic, Sinisa

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