Mikael Widersten
Professor i biokemi vid Institutionen för kemi - BMC; Biokemi; Widersten grupp
- Telefon:
- 018-471 49 92
- Mobiltelefon:
- 073-695 18 63
- E-post:
- Mikael.Widersten@kemi.uu.se
- Besöksadress:
- Husargatan 3
752 37 Uppsala - Postadress:
- Box 576
75123 Uppsala
- Akademiska meriter:
- FD, docent i biokemi
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Kort presentation
Professor i biokemi (Molekylär katalys). Min forskning syftar till att öka förståelsen av struktur/funktionssamband i enzymer för att kunna tillämpa dessa vid utveckling av nya och användbara biokatalysatorer.
Biografi
Publikationer
Senaste publikationer
- Structural enzymology studies with the substrate3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD (2024)
- Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted Ketones and Aldehydes (2023)
- Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity (2023)
- Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics (2023)
- Facile Synthesis of 2-Hydroxyacetophenone from Racemic Styrene Oxide Catalyzed by Engineered Enzymes (2022)
Alla publikationer
Artiklar
- Structural enzymology studies with the substrate3S-hydroxybutanoyl-CoA: bifunctional MFE1 is a less efficient dehydrogenase than monofunctional HAD (2024)
- Engineered Aldolases Catalyzing Stereoselective Aldol Reactions Between Aryl-Substituted Ketones and Aldehydes (2023)
- Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity (2023)
- Structures of lactaldehyde reductase, FucO, link enzyme activity to hydrogen bond networks and conformational dynamics (2023)
- Facile Synthesis of 2-Hydroxyacetophenone from Racemic Styrene Oxide Catalyzed by Engineered Enzymes (2022)
- Structure and Mechanism of a Cold-Adapted Bacterial Lipase (2022)
- The Role of Substrate-Coenzyme Crosstalk in Determining Turnover Rates in Rhodococcus ruber Alcohol Dehydrogenase (2020)
- Engineering aldolases for asymmetric synthesis (2020)
- Chemical and Biochemical Approaches for the Synthesis of Substituted Dihydroxybutanones and Di-, and Tri-Hydroxypentanones (2019)
- Synthesis of substrates for aldolase-catalyzed reactions (2018)
- Directed Evolution of Alcohol Dehydrogenase for Improved Stereoselective Redox Transformations of 1-Phenylethane-1,2-Diol and Its Corresponding Acyloin (2018)
- Epoxide Hydrolysis as a Model System for Understanding Flux Through a Branched Reaction Scheme (2018)
- New Stereoselective Biocatalysts for Carboligation and Retro-Aldol Cleavage Reactions Derived from D-Fructose 6-Phosphate Aldolase (2018)
- 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 (2018)
- Crystal structure and pH-dependent allosteric regulation of human β-ureidopropionase, an enzyme involved in anticancer drug metabolism (2018)
- Relaxation of Nonproductive Binding and Increased Rate of Coenzyme Release in an Alcohol Dehydrogenase Increases Turnover With a Non-Preferred Alcohol Enantiomer (2017)
- Conformational Diversity and Enantioconvergence in Potato Epoxide Hydrolase 1 (2016)
- Laboratory evolved enzymes provide snapshots of the development of enantioconvergence in enzyme-catalyzed epoxide hydrolysis (2016)
- Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA) (2016)
- Expanding the catalytic triad in epoxide hydrolases and related enzymes (2015)
- Directed evolution on FucO - structural explanations for changes in substrate scope (2015)
- Design of a PDZbody, a bivalent binder of the E6 protein from human papillomavirus (2015)
- A micro-plate format assay for real-time screening for new aldolases accepting aryl-substituted acceptor substrates (2015)
- Substrate scope and selectivity in offspring to an enzyme subjected to directed evolution (2014)
- Kinetic characterization of Rhodococcus ruber DSM 44541 alcohol dehydrogenase A (2014)
- Protein engineering for development of new hydrolytic biocatalysts (2014)
- Stereoselective oxidation of aryl-substituted vicinal diols into chiral α-hydroxy aldehydes by re-engineered propanediol oxidoreductase (2013)
- Obtaining optical purity for product diols in enzyme-catalyzed epoxide hydrolysis (2012)
- One-step enzyme extraction and immobilization for biocatalysis applications (2011)
- Functional characterization of a stereospecific diol dehydrogenase, FucO, from Escherichia coli (2010)
- Modification of substrate specificity resulted in an epoxide hydrolase with shifted enantiopreference for (2,3-epoxypropyl)benzene (2010)
- Mutations in salt-bridging residues at the interface of the core and lid domains of epoxide hydrolase StEH1 affect regioselectivity, protein stability and hysteresis (2010)
- Temperature and pH dependence of enzyme catalyzed hydrolysis of trans-methylstyrene oxide (2010)
- Deep eutectic solvents (DESs) are viable cosolvents for enzyme-catalyzed epoxide hydrolysis (2010)
- Structure-function relationships of epoxide hydrolases and their potential use in biocatalysis (2010)
- Substrate-dependent hysteretic behavior in StEH1-catalyzed hydrolysis of styrene oxide derivatives (2008)
- Removal of distal protein-water hydrogen bonds in a plant epoxide hydrolase increases catalytic turnover but decreases thermostability (2008)
- Active site of epoxide hydrolases revisited (2007)
- Implications for an Ionized Alkyl-Enzyme Intermediate during StEH1-Catalyzed trans-Stilbene Oxide Hydrolysis (2006)
- X-ray structure of potato epoxide hydrolase sheds light on its substrate specificity (2006)
- Catalysis of potato epoxide hydrolase, StEH1 (2005)
- The Saccharomyces cerevisiae ORF YNR064c protein has characteristics of an 'orphaned' epoxide hydrolase (2005)
- Isolation of novel single-chain Cro proteins targeted for binding to the bcl-2 transcription initiation site by repertoire selection and subunit combinatorics (2005)
- Repertoire selection of variant single-chain Cro (2004)
- Amino acid residue 247 in canine sulphotransferase SULT1D1: a new determinant of substrate selectivity. (2004)
- Inhibition of glutathione S-transferases by antimalarial drugs (2002)
- Yeast glyoxalase I is a monomeric enzyme with two active sites (2001)
- Chlorine kinetic isotope effects on the haloalkane dehalogenase reaction (2001)
- Proposed reductive metabolism of artemisinin by glutathione transferases in vitro (2001)
- Examination of the transcription factor NtcA-binding motif by in vitro selection of DNA sequences from a random library (2000)
- Functional expression and affinity selection of single-chain Cro by phage display: isolation of novel DNA-binding proteins (2000)
- An approach to optimizing the active site in a glutathione transferase by evolution in vitro (1999)
- Structural determinants in domain II of human glutathione transferase M2-2 govern the characteristic activities with aminochrome, 2-cyano-1,3-dimethyl-1-nitrosoguanidine, and 1,2-dichloro-4-nitrobenzene (1999)
- Hydrophobic sequences can substitute for the wild-type N-terminal sequence of cystatin A (stefin A) in tight binding to cysteine proteinases. Selection of high-affinity N-terminal region variants by phage display (1999)
- Structure-activity relationships and thermal stability of human glutathione transferase P1-1 governed by the H-site residue 105 (1998)
- Differences in the catalytic efficiencies of allelic variants of glutathione transferase P1-1 towards carcinogenic diol epoxides of polycyclic aromatic hydrocarbons (1998)
- Heterologous Expression in Escherichia coli of SolubleActive-Site Random Mutants of Haloalkane Dehalogenase from Xanthobacter autotrophicus GJ10 by Coexpression of Molecular Chaperonins GroEL/ES (1998)
- Glutathione transferases catalyse the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes (1997)
- Mechanism-based phage display selection of active-site mutants of human glutathione transferase A1-1 catalyzing SNAr reactions (1997)
- Conjugation of highly reactive aflatoxin B1 exo-8,9-epoxide catalyzed by rat and human glutathione transferases: Estimation of kinetic parameters (1997)
- Human class Mu glutathione transferases, in particular isoenzyme M2-2,catalyze detoxication of the dopamine metabolite aminochrome (1997)
- Glutathione conjugation of bay- and fjord-region diol epoxides of polycyclic aromatic hydrocarbons by glutathione transferases M1-1 and P1-1 (1997)
- Involvement of the carboxyl groups of glutathione in the catalytic mechanism of human glutathione transferase A1-1 (1996)
- Optimized heterologous expression of the polymorphic human glutathione transferase M1-1 based on silent mutations in the corresponding cDNA (1996)
- FUNCTIONAL-SIGNIFICANCE OF ARGININE-15 IN THE ACTIVE-SITE OF HUMAN CLASS-ALPHA GLUTATHIONE TRANSFERASE A1-1 (1995)
- High-level bacterial expression of human glutathione transferase P1-1 encoded by semisynthetic DNA (1995)
- Glutathione transferases with novel active sites isolated by phage display from a library of random mutants (1995)
- Generation of a Ni(II) binding site by introduction of a histidine cluster in the structure of human glutathione transferase A1-1 (1995)
- Detoxication of base propenals and other α,β-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases (1994)
- Engineering of a metal coordinating site into human glutathione transferase M1-1 based on immobilized metal ion affinity chromatography of homologous rat enzymes (1994)
- A comparison of the enzymatic and physicochemical properties of human glutathione transferase M4-4 and three other human Mu class enzymes (1994)
- Co-variation of glutathione transferase expression and cytostatic drug resistance in HeLa cells: establishment of class Mu glutathione transferase M3-3 as the dominating isoenzyme (1994)
- Contribution of amino acid residue 208 in the hydrophobic binding site to the catalytic mechanism of human glutathione transferase A 1-1 (1994)
- NOMENCLATURE FOR HUMAN GLUTATHIONE TRANSFERASES (1992)
- DESIGN OF 2 CHIMERIC HUMAN RAT CLASS ALPHA-GLUTATHIONE TRANSFERASES FOR PROBING THE CONTRIBUTION OF C-TERMINAL SEGMENTS OF PROTEIN-STRUCTURE TO THE CATALYTIC PROPERTIES (1992)
- Contribution of five amino acid residues in the glutathione-binding site to the function of human glutathione transferase P1-1 (1992)
- A structural role of histidine 15 in juman gutathione transferase M1-1, an amino acid residue conserved in class Mu enzymes (1992)
- CYSTEINE RESIDUES ARE NOT ESSENTIAL FOR THE CATALYTIC ACTIVITY OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE M1A-1A (1991)
- HETEROLOGOUS EXPRESSION OF THE ALLELIC VARIANT MU-CLASS GLUTATHIONE TRANSFERASES μ AND TRANSFERASES ψ (1991)
- DIFFERENCES AMONG HUMAN TUMOR-CELL LINES IN THE EXPRESSION OF GLUTATHIONE TRANSFERASES AND OTHER GLUTATHIONE-LINKED ENZYMES (1990)
- Characterization and structure determination of human β-ureidopropionase reveal pH-dependent regulation by ligand-induced changes in oligomerization
