Widerstens grupp

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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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, 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
• Ladda ner fulltext (pdf) av High-throughput selection of (new) enzymes: phage display-mediated isolation of alkyl halide hydrolases from a library of active-site mutated epoxide hydrolases

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
• Ladda ner fulltext (pdf) av Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes

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 J.; Xiong, Ruisheng et al.

Ingår i Catalysis Science & Technology, 2023

• DOI för Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted 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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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
• Ladda ner fulltext (pdf) av Structure and Mechanism of a Cold-Adapted Bacterial Lipase

Engineering aldolases for asymmetric synthesis

Widersten, Mikael

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

• DOI för Engineering aldolases for asymmetric synthesis

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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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

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

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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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
• Ladda ner fulltext (pdf) av 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

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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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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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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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

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
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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

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

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

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

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

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

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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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

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

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

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

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

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

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

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, 2004

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

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

Inhibition of glutathione S-transferases by antimalarial drugs: Possible implications for circumventing anticancer drug resistance

Mukanganyama, Stanley; Widersten, Mikael; Naik, Yogeshkumar S.; Mannervik, Bengt et al.

Ingår i Int J Cancer, s. 700-705, 2002

• DOI för Inhibition of glutathione S-transferases by antimalarial drugs: Possible implications for circumventing anticancer drug resistance

Yeast glyoxalase I is a monomeric enzyme with two active sites

Frickel, EM; Jemth, P; Widersten, M; Mannervik, B

Ingår i Journal of Biological Chemistry, s. 1845-1849, 2001