Widerstens grupp

Structural enzymological studies of multifunctional enzyme, type-1 (MFE1) with the 2E-decenoyl-CoA and 2E,4E-decadienoyl-CoA substrates: The regeneration of the dehydrogenase catalytic site is the rate limiting step of its combined reactions

Sridhar, Shruthi; Schmitz, Werner; Widersten, Mikael; Wierenga, Rik K. et al.

Ingår i Journal of Structural Biology, 2026

• DOI för Structural enzymological studies of multifunctional enzyme, type-1 (MFE1) with the 2E-decenoyl-CoA and 2E,4E-decadienoyl-CoA substrates: The regeneration of the dehydrogenase catalytic site is the rate limiting step of its combined reactions
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Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors

Gulyás, Kinga; Zhou, Liping; Salamonsen, Daniel; Prester, Andreas et al.

Ingår i Communications Chemistry, 2025

• DOI för Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors
• Ladda ner fulltext (pdf) av Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors

High-throughput selection of (new) enzymes: phage display-mediated isolation of alkyl halide hydrolases from a library of active-site mutated epoxide hydrolases

Blazic, Marija; Gautier, Candice; Norberg, Thomas; Widersten, Mikael

Ingår i Faraday discussions, s. 115-126, 2024

• DOI för High-throughput selection of (new) enzymes: phage display-mediated isolation of alkyl halide hydrolases from a library of active-site mutated epoxide hydrolases
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Structural enzymology studies with the substrate3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD

Sridhar, Shruthi; Kiema, Tiila-Riikka Kiema; Schmitz, Werner; Widersten, Mikael et al.

Ingår i FEBS Open Bio, s. 655-674, 2024

• DOI för Structural enzymology studies with the substrate3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD
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Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes

Hebert, Hans; Sönmez, Eda; Purhonen, Pasi; Widersten, Mikael

Ingår i Structure, s. 1322-13260000, 2024

• DOI för Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes
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Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity

Sridhar, Shruthi; Zavarise, Alberto; Kiema, Tiila-Riikka; Dalwani, Subhadra et al.

Ingår i IUCrJ, s. 437-447, 2023

• DOI för Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity
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Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics

Zavarise, Alberto; Sridhar, Shruthi; Kiema, Tiila-Riikka; Wierenga, Rikkert K. et al.

Ingår i The FEBS Journal, s. 465-481, 2023

• DOI för Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics
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Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted Ketones and Aldehydes

Cornelius Chukwu, Eugenia; Bartl, Michael; Persson, Louise; Xiong, Ruisheng et al.

Ingår i Catalysis Science & Technology, s. 4978-4987, 2023

• DOI för Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted Ketones and Aldehydes
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Facile Synthesis of 2-Hydroxyacetophenone from Racemic Styrene Oxide Catalyzed by Engineered Enzymes

Söderlund, Isac; Tjärnhage, Elias; Hamnevik, Emil; Widersten, Mikael

Ingår i Biotechnology letters, s. 985-990, 2022

• DOI för Facile Synthesis of 2-Hydroxyacetophenone from Racemic Styrene Oxide Catalyzed by Engineered Enzymes
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Structure and Mechanism of a Cold-Adapted Bacterial Lipase

van der Ent, Florian; Lund, Bjarte A.; Svalberg, Linn; Purg, Miha et al.

Ingår i Biochemistry, s. 933-942, 2022

• DOI för Structure and Mechanism of a Cold-Adapted Bacterial Lipase
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The Role of Substrate-Coenzyme Crosstalk in Determining Turnover Rates in Rhodococcus ruber Alcohol Dehydrogenase

Enugala, Thilak Reddy; Corbella Morató, Marina; Kamerlin, Shina C. L.; Widersten, Mikael

Ingår i ACS Catalysis, s. 9115-9128, 2020

• DOI för The Role of Substrate-Coenzyme Crosstalk in Determining Turnover Rates in Rhodococcus ruber Alcohol Dehydrogenase
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Engineering aldolases for asymmetric synthesis

Widersten, Mikael

Ingår i Methods in Enzymology, s. 149-167, 2020

• DOI för Engineering aldolases for asymmetric synthesis

Chemical and Biochemical Approaches for the Synthesis of Substituted Dihydroxybutanones and Di-, and Tri-Hydroxypentanones

Al-Smadi, Derar; Enugala, Thilak Reddy; Kessler, Vadim; Mhasal, Anil Rhanu et al.

Ingår i Journal of Organic Chemistry, s. 6982-6991, 2019

• DOI för Chemical and Biochemical Approaches for the Synthesis of Substituted Dihydroxybutanones and Di-, and Tri-Hydroxypentanones

Synthesis of substrates for aldolase-catalyzed reactions: A comparison of methods for the synthesis of substituted phenylacetaldehydes

Al-Smadi, Derar; Enugala, Thilak Reddy; Norberg, Thomas; Kihlberg, Jan et al.

Ingår i Synlett, s. 1187-1190, 2018

• DOI för Synthesis of substrates for aldolase-catalyzed reactions: A comparison of methods for the synthesis of substituted phenylacetaldehydes

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

Maurer, Dirk; Enugala, Thilak Reddy; Hamnevik, Emil; Bauer, Paul et al.

Ingår i ACS Catalysis, s. 7526-7538, 2018

• DOI för 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
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Crystal structure and pH-dependent allosteric regulation of human β-ureidopropionase, an enzyme involved in anticancer drug metabolism

Maurer, Dirk; Lohkamp, Bernhard; Krumpel, Michael; Widersten, Mikael et al.

Ingår i Biochemical Journal, s. 2395-2416, 2018

• DOI för Crystal structure and pH-dependent allosteric regulation of human β-ureidopropionase, an enzyme involved in anticancer drug metabolism

New Stereoselective Biocatalysts for Carboligation and Retro-Aldol Cleavage Reactions Derived from D-Fructose 6-Phosphate Aldolase

Ma, Huan; Engel, Sarah; Enugala, Thilak Reddy; Al-Smadi, Derar et al.

Ingår i Biochemistry, s. 5877-5885, 2018

• DOI för New Stereoselective Biocatalysts for Carboligation and Retro-Aldol Cleavage Reactions Derived from D-Fructose 6-Phosphate Aldolase

Epoxide Hydrolysis as a Model System for Understanding Flux Through a Branched Reaction Scheme

Janfalk Carlsson, Åsa; Bauer, Paul; Dobritzsch, Doreen; Kamerlin, Shina C Lynn et al.

Ingår i IUCrJ, s. 269-282, 2018

• DOI för Epoxide Hydrolysis as a Model System for Understanding Flux Through a Branched Reaction Scheme
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Directed Evolution of Alcohol Dehydrogenase for Improved Stereoselective Redox Transformations of 1-Phenylethane-1,2-Diol and Its Corresponding Acyloin

Hamnevik, Emil; Maurer, Dirk; Enugala, Thilak Reddy; Chu, Thao et al.

Ingår i Biochemistry, s. 1059-1062, 2018

• DOI för Directed Evolution of Alcohol Dehydrogenase for Improved Stereoselective Redox Transformations of 1-Phenylethane-1,2-Diol and Its Corresponding Acyloin

Relaxation of Nonproductive Binding and Increased Rate of Coenzyme Release in an Alcohol Dehydrogenase Increases Turnover With a Non-Preferred Alcohol Enantiomer

Hamnevik, Emil; Enugala, Thilak Reddy; Maurer, Dirk; Ntuku, Siphosethu et al.

Ingår i The FEBS Journal, s. 3895-3914, 2017

• DOI för Relaxation of Nonproductive Binding and Increased Rate of Coenzyme Release in an Alcohol Dehydrogenase Increases Turnover With a Non-Preferred Alcohol Enantiomer
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Laboratory evolved enzymes provide snapshots of the development of enantioconvergence in enzyme-catalyzed epoxide hydrolysis

Janfalk Carlsson, Åsa; Bauer, Paul; Dobritzsch, Doreeen; Nilsson, Mikael et al.

Ingår i ChemBioChem, s. 1693-1697, 2016

• DOI för Laboratory evolved enzymes provide snapshots of the development of enantioconvergence in enzyme-catalyzed epoxide hydrolysis
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Conformational Diversity and Enantioconvergence in Potato Epoxide Hydrolase 1

Bauer, Paul; Janfalk Carlsson, Åsa; Amrein, Beat A.; Dobritzsch, Doreen et al.

Ingår i Organic and biomolecular chemistry, s. 5639-5651, 2016

• DOI för Conformational Diversity and Enantioconvergence in Potato Epoxide Hydrolase 1
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Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)

Ma, Huan; Szeler, Klaudia; Kamerlin, Shina Caroline Lynn; Widersten, Mikael

Ingår i Chemical Science, s. 1415-1421, 2016

• DOI för Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)
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Directed evolution on FucO - structural explanations for changes in substrate scope

Dahlström, Kathe M.; Blikstad, Cecilia; Widersten, Mikael; Salminen, Tiina A.

Ingår i Protein Science, s. 199-200, 2015

Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus

Karlsson, O. Andreas; Ramirez, Juan; Öberg, Daniel; Malmqvist, Tony et al.

Ingår i Scientific Reports, 2015

• DOI för Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus
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Expanding the catalytic triad in epoxide hydrolases and related enzymes

Amrein, Beat A.; Bauer, Paul; Duarte, Fernanda; Janfalk Carlsson, Åsa et al.

Ingår i ACS Catalysis, s. 5702-5713, 2015

• DOI för Expanding the catalytic triad in epoxide hydrolases and related enzymes
• Ladda ner fulltext (pdf) av Expanding the catalytic triad in epoxide hydrolases and related enzymes

A micro-plate format assay for real-time screening for new aldolases accepting aryl-substituted acceptor substrates

Ma, Huan; Enugala, Thilak Reddy; Widersten, Mikael

Ingår i ChemBioChem, s. 2595-2598, 2015

• DOI för A micro-plate format assay for real-time screening for new aldolases accepting aryl-substituted acceptor substrates

Substrate scope and selectivity in offspring to an enzyme subjected to directed evolution

Blikstad, Cecilia; Dahlström, Käthe; Salminen, Tiina; Widersten, Mikael

Ingår i The FEBS Journal, s. 2387-2398, 2014

• DOI för Substrate scope and selectivity in offspring to an enzyme subjected to directed evolution

Protein engineering for development of new hydrolytic biocatalysts

Widersten, Mikael

Ingår i Current opinion in chemical biology, s. 42-47, 2014

• DOI för Protein engineering for development of new hydrolytic biocatalysts
• Ladda ner fulltext (pdf) av Protein engineering for development of new hydrolytic biocatalysts

Kinetic characterization of Rhodococcus ruber DSM 44541 alcohol dehydrogenase A

Hamnevik, Emil; Blikstad, Cecilia; Norrehed, Sara; Widersten, Mikael

Ingår i Journal of Molecular Catalysis B, s. 68-78, 2014

• DOI för Kinetic characterization of Rhodococcus ruber DSM 44541 alcohol dehydrogenase A

Stereoselective oxidation of aryl-substituted vicinal diols into chiral α-hydroxy aldehydes by re-engineered propanediol oxidoreductase

Blikstad, Cecilia; Dahlström, Kärthe M.; Salminen, Tiina A.; Widersten, Mikael

Ingår i ACS Catalysis, s. 3016-3025, 2013

• DOI för Stereoselective oxidation of aryl-substituted vicinal diols into chiral α-hydroxy aldehydes by re-engineered propanediol oxidoreductase

Obtaining optical purity for product diols in enzyme-catalyzed epoxide hydrolysis: contributions from changes in both enantio- and regioselectivity

Janfalk Carlsson, Åsa; Bauer, Paul; Ma, Huan; Widersten, Mikael

Ingår i Biochemistry, s. 7627-7637, 2012

• DOI för Obtaining optical purity for product diols in enzyme-catalyzed epoxide hydrolysis: contributions from changes in both enantio- and regioselectivity

Exploring the active site of tripeptidyl-peptidase II through studies of pH dependence of reaction kinetics

Eklund, Sandra; Lindås, Ann-Christin; Hamnevik, Emil; Widersten, Mikael et al.

Ingår i Biochimica et Biophysica Acta - Proteins and Proteomics, s. 561-570, 2012

• DOI för Exploring the active site of tripeptidyl-peptidase II through studies of pH dependence of reaction kinetics

One-step enzyme extraction and immobilization for biocatalysis applications

Cassimjee, Karim Engelmark; Kourist, Robert; Lindberg, Diana; Wittrup Larsen, Marianne et al.

Ingår i Biotechnology Journal, s. 463-469, 2011

• DOI för One-step enzyme extraction and immobilization for biocatalysis applications

Functional characterization of a stereospecific diol dehydrogenase, FucO, from Escherichia coli: substrate specificity, pH dependence, kinetic isotope effects and influence of solvent viscosity

Blikstad, Cecilia; Widersten, Mikael

Ingår i Journal of Molecular Catalysis B, s. 148-155, 2010

• DOI för Functional characterization of a stereospecific diol dehydrogenase, FucO, from Escherichia coli: substrate specificity, pH dependence, kinetic isotope effects and influence of solvent viscosity

Temperature and pH dependence of enzyme catalyzed hydrolysis of trans-methylstyrene oxide: a unifying kinetic model for observed hysteresis, cooperativity and regioselectivity

Lindberg, Diana; de la Fuente Revenga, Mario; Widersten, Mikael

Ingår i Biochemistry, s. 2297-2304, 2010

• DOI för Temperature and pH dependence of enzyme catalyzed hydrolysis of trans-methylstyrene oxide: a unifying kinetic model for observed hysteresis, cooperativity and regioselectivity

Structure-function relationships of epoxide hydrolases and their potential use in biocatalysis

Widersten, Mikael; Gurell, Ann; Lindberg, Diana

Ingår i Biochimica et Biophysica Acta, s. 316-326, 2010

• DOI för Structure-function relationships of epoxide hydrolases and their potential use in biocatalysis

Mutations in salt-bridging residues at the interface of the core and lid domains of epoxide hydrolase StEH1 affect regioselectivity, protein stability and hysteresis

Lindberg, Diana; Ahmad, Shabbir; Widersten, Mikael

Ingår i Archives of Biochemistry and Biophysics, s. 165-173, 2010

• DOI för Mutations in salt-bridging residues at the interface of the core and lid domains of epoxide hydrolase StEH1 affect regioselectivity, protein stability and hysteresis

Deep eutectic solvents (DESs) are viable cosolvents for enzyme-catalyzed epoxide hydrolysis

Lindberg, Diana; de la Fuente Revenga, Mario; Widersten, Mikael

Ingår i Journal of Biotechnology, s. 169-171, 2010

• DOI för Deep eutectic solvents (DESs) are viable cosolvents for enzyme-catalyzed epoxide hydrolysis

Modification of substrate specificity resulted in an epoxide hydrolase with shifted enantiopreference for (2,3-epoxypropyl)benzene

Gurell, Ann; Widersten, Mikael

Ingår i ChemBioChem, s. 1422-1429, 2010

• DOI för Modification of substrate specificity resulted in an epoxide hydrolase with shifted enantiopreference for (2,3-epoxypropyl)benzene

Substrate-dependent hysteretic behavior in StEH1-catalyzed hydrolysis of styrene oxide derivatives

Lindberg, Diana; Gogoll, Adolf; Widersten, Mikael

Ingår i The FEBS Journal, s. 6309-6320, 2008

• DOI för Substrate-dependent hysteretic behavior in StEH1-catalyzed hydrolysis of styrene oxide derivatives

Removal of distal protein-water hydrogen bonds in a plant epoxide hydrolase increases catalytic turnover but decreases thermostability

Thomaeus, Ann; Naworyta, Agata; Mowbray, Sherry L.; Widersten, Mikael

Ingår i Protein Science, s. 1275-1284, 2008

• DOI för Removal of distal protein-water hydrogen bonds in a plant epoxide hydrolase increases catalytic turnover but decreases thermostability
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Active site of epoxide hydrolases revisited: A noncanonical residue in potato StEH1 promotes both formation and breakdown of the alkylenzyme intermediate

Thomaeus, Ann; Carlsson, Jens; Åqvist, Johan; Widersten, Mikael

Ingår i Biochemistry, s. 2466-2479, 2007

• DOI för Active site of epoxide hydrolases revisited: A noncanonical residue in potato StEH1 promotes both formation and breakdown of the alkylenzyme intermediate

X-ray structure of potato epoxide hydrolase sheds light on its substrate specificity

Mowbray, Sherry L.; Elfström, Lisa; Ahlgren, Kerstin; Andersson, Evalena et al.

Ingår i Protein Science, s. 1628-1637, 2006

• DOI för X-ray structure of potato epoxide hydrolase sheds light on its substrate specificity

Implications for an Ionized Alkyl-Enzyme Intermediate during StEH1-Catalyzed trans-Stilbene Oxide Hydrolysis

Elfström, Lisa; Widersten, Mikael

Ingår i Biochemistry, s. 205-212, 2006

• DOI för Implications for an Ionized Alkyl-Enzyme Intermediate during StEH1-Catalyzed trans-Stilbene Oxide Hydrolysis

Isolation of novel single-chain Cro proteins targeted for binding to the bcl-2 transcription initiation site by repertoire selection and subunit combinatorics

Jonas, Kristina; Van Der Vries, Erhard; Nilsson, Mikael T.I.; Widersten, Mikael

Ingår i Protein Engineering Design & Selection, s. 537-546, 2005

• DOI för Isolation of novel single-chain Cro proteins targeted for binding to the bcl-2 transcription initiation site by repertoire selection and subunit combinatorics

The Saccharomyces cerevisiae ORF YNR064c protein has characteristics of an 'orphaned' epoxide hydrolase

Elfström, Lisa; Widersten, Mikael

Ingår i Biochimica et Biophysica Acta - Proteins and Proteomics, s. 213-221, 2005

• DOI för The Saccharomyces cerevisiae ORF YNR064c protein has characteristics of an 'orphaned' epoxide hydrolase

Catalysis of potato epoxide hydrolase, StEH1

Elfström, Lisa; Widersten, Mikael

Ingår i Biochemical Journal, s. 633-640, 2005

• DOI för Catalysis of potato epoxide hydrolase, StEH1

Repertoire selection of variant single-chain Cro: towards directed DNA-binding specificity of helix-turn-helix proteins

Nilsson, Mikael T.I.; Widersten, Mikael

Ingår i Biochemistry, s. 12038-12047, 2004

• DOI för Repertoire selection of variant single-chain Cro: towards directed DNA-binding specificity of helix-turn-helix proteins

Amino acid residue 247 in canine sulphotransferase SULT1D1: a new determinant of substrate selectivity

Tsoi, Carrie; Widersten, Mikael; Morgenstern, Ralf; Swedmark, Stellan

Ingår i Biochemical Journal, s. 687-692, 2004

• DOI för Amino acid residue 247 in canine sulphotransferase SULT1D1: a new determinant of substrate selectivity