Widersten Group
Enzymology and directed protein evolution
Enzyme catalysts are characterized by an unprecedented specificity for reactant molecules that will be acted upon. Often only a specific stereoisomer of a chiral molecule will be efficiently converted by a particular enzyme. Such specificity is of high value if applied to synthesis of chiral organic compounds where product purity is essential.
We study structure/function relationships in enzymes and use what we learn for the development of new and useful biocatalysts for specific and efficient catalysis of reactions generating chiral and pro-chiral product molecules.
Group members
Publications
Part of FEBS Open Bio, p. 655-674, 2024
- DOI for Structural enzymology studies with the substrate3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD
- Download full text (pdf) of Structural enzymology studies with the substrate3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD
Part of Faraday discussions, 2024
- DOI for High-throughput selection of (new) enzymes: phage display-mediated isolation of alkyl halide hydrolases from a library of active-site mutated epoxide hydrolases
- Download full text (pdf) of High-throughput selection of (new) enzymes: phage display-mediated isolation of alkyl halide hydrolases from a library of active-site mutated epoxide hydrolases
Part of Structure, p. 1322-13260000, 2024
- DOI for Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes
- Download full text (pdf) of Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes
Part of The FEBS Journal, p. 465-481, 2023
Part of Catalysis Science & Technology, 2023
Part of IUCrJ, p. 437-447, 2023
- DOI for Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity
- Download full text (pdf) of Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity
Facile Synthesis of 2-Hydroxyacetophenone from Racemic Styrene Oxide Catalyzed by Engineered Enzymes
Part of Biotechnology letters, p. 985-990, 2022
Structure and Mechanism of a Cold-Adapted Bacterial Lipase
Part of Biochemistry, p. 933-942, 2022
Engineering aldolases for asymmetric synthesis
Part of Methods in Enzymology, p. 149-167, 2020
Part of ACS Catalysis, p. 9115-9128, 2020
Part of Journal of Organic Chemistry, p. 6982-6991, 2019
Part of Synlett, p. 1187-1190, 2018
Part of Biochemical Journal, p. 2395-2416, 2018
Part of Biochemistry, p. 5877-5885, 2018
Epoxide Hydrolysis as a Model System for Understanding Flux Through a Branched Reaction Scheme
Part of IUCrJ, p. 269-282, 2018
Part of Biochemistry, p. 1059-1062, 2018
Part of ACS Catalysis, p. 7526-7538, 2018
- DOI for Stereo- and Regioselectivity in Catalyzed Transformation of a 1,2-Disubstituted Vicinal Diol and the Corresponding Diketone by Wild Type and Laboratory Evolved Alcohol Dehydrogenases
- Download full text (pdf) of Stereo- and Regioselectivity in Catalyzed Transformation of a 1,2-Disubstituted Vicinal Diol and the Corresponding Diketone by Wild Type and Laboratory Evolved Alcohol Dehydrogenases
Part of The FEBS Journal, p. 3895-3914, 2017
- DOI for Relaxation of Nonproductive Binding and Increased Rate of Coenzyme Release in an Alcohol Dehydrogenase Increases Turnover With a Non-Preferred Alcohol Enantiomer
- Download full text (pdf) of Relaxation of Nonproductive Binding and Increased Rate of Coenzyme Release in an Alcohol Dehydrogenase Increases Turnover With a Non-Preferred Alcohol Enantiomer
Conformational Diversity and Enantioconvergence in Potato Epoxide Hydrolase 1
Part of Organic and biomolecular chemistry, p. 5639-5651, 2016
Part of Chemical Science, p. 1415-1421, 2016
Part of ChemBioChem, p. 1693-1697, 2016
Directed evolution on FucO - structural explanations for changes in substrate scope
Part of Protein Science, p. 199-200, 2015
Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus
Part of Scientific Reports, 2015
Part of ChemBioChem, p. 2595-2598, 2015
Expanding the catalytic triad in epoxide hydrolases and related enzymes
Part of ACS Catalysis, p. 5702-5713, 2015
Protein engineering for development of new hydrolytic biocatalysts
Part of Current opinion in chemical biology, p. 42-47, 2014
Kinetic characterization of Rhodococcus ruber DSM 44541 alcohol dehydrogenase A
Part of Journal of Molecular Catalysis B, p. 68-78, 2014
Substrate scope and selectivity in offspring to an enzyme subjected to directed evolution
Part of The FEBS Journal, p. 2387-2398, 2014
Part of ACS Catalysis, p. 3016-3025, 2013
Part of Biochemistry, p. 7627-7637, 2012
Part of Biochimica et Biophysica Acta - Proteins and Proteomics, p. 561-570, 2012
One-step enzyme extraction and immobilization for biocatalysis applications
Part of Biotechnology Journal, p. 463-469, 2011
Part of Journal of Molecular Catalysis B, p. 148-155, 2010
Part of Biochemistry, p. 2297-2304, 2010
Part of Archives of Biochemistry and Biophysics, p. 165-173, 2010
Deep eutectic solvents (DESs) are viable cosolvents for enzyme-catalyzed epoxide hydrolysis
Part of Journal of Biotechnology, p. 169-171, 2010
Structure-function relationships of epoxide hydrolases and their potential use in biocatalysis
Part of Biochimica et Biophysica Acta, p. 316-326, 2010
Part of ChemBioChem, p. 1422-1429, 2010
Part of Protein Science, p. 1275-1284, 2008
- DOI for Removal of distal protein-water hydrogen bonds in a plant epoxide hydrolase increases catalytic turnover but decreases thermostability
- Download full text (pdf) of Removal of distal protein-water hydrogen bonds in a plant epoxide hydrolase increases catalytic turnover but decreases thermostability
Substrate-dependent hysteretic behavior in StEH1-catalyzed hydrolysis of styrene oxide derivatives
Part of The FEBS Journal, p. 6309-6320, 2008
Part of Biochemistry, p. 2466-2479, 2007
Part of Biochemistry, p. 205-212, 2006
X-ray structure of potato epoxide hydrolase sheds light on its substrate specificity
Part of Protein Science, p. 1628-1637, 2006
Catalysis of potato epoxide hydrolase, StEH1
Part of Biochemical Journal, p. 633-640, 2005
Part of Biochimica et Biophysica Acta - Proteins and Proteomics, p. 213-221, 2005
Part of Protein Engineering Design & Selection, p. 537-546, 2005
Part of Biochemical Journal, 2004
Part of Biochemistry, p. 12038-12047, 2004
Part of Int J Cancer, p. 700-705, 2002
Yeast glyoxalase I is a monomeric enzyme with two active sites
Part of Journal of Biological Chemistry, p. 1845-1849, 2001