Werner Hummel

Summary

Country: Germany

Publications

  1. ncbi request reprint Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis
    Werner Hummel
    Institut für Enzymtechnologie der Heinrich Heine Universität, Forschungszentrum Julich, Wilhelm Johnen Str, D 52426 Jülich, Germany
    Biotechnol Lett 25:51-4. 2003
  2. doi request reprint Strategies for regeneration of nicotinamide coenzymes emphasizing self-sufficient closed-loop recycling systems
    Werner Hummel
    Institute of Molecular Enzyme Technology at the Heinrich Heine University of Düsseldorf, Research Centre Julich, Stetternicher Forst, 52426 Julich, Germany Electronic address
    J Biotechnol 191:22-31. 2014
  3. ncbi request reprint An efficient and selective enzymatic oxidation system for the synthesis of enantiomerically pure D-tert-leucine
    Werner Hummel
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, im Forschungszentrum Jülich, 52426 Julich, Germany
    Org Lett 5:3649-50. 2003
  4. doi request reprint Purification, cloning, and overexpression of an alcohol dehydrogenase from Nocardia globerula reducing aliphatic ketones and bulky ketoesters
    Julia Parkot
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungzentrum Jülich, Stetternicher Forst, 52426, Julich, Germany
    Appl Microbiol Biotechnol 86:1813-20. 2010
  5. doi request reprint Regeneration of nicotinamide coenzymes: principles and applications for the synthesis of chiral compounds
    Andrea Weckbecker
    Institute of Molecular Enzyme Technology, Heinrich Heine University of Dusseldorf, Research Centre Julich, Stetternicher Forst, 52426, Julich, Germany
    Adv Biochem Eng Biotechnol 120:195-242. 2010
  6. pmc Crystallization and preliminary crystallographic analysis of a flavoprotein NADH oxidase from Lactobacillus brevis
    Mutlu Kuzu
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Centre Julich, 52426 Julich, Germany
    Acta Crystallogr Sect F Struct Biol Cryst Commun 61:528-30. 2005
  7. ncbi request reprint Improved synthesis of chiral alcohols with Escherichia coli cells co-expressing pyridine nucleotide transhydrogenase, NADP+-dependent alcohol dehydrogenase and NAD+-dependent formate dehydrogenase
    Andrea Weckbecker
    Institut für Molekulare Enzymtechnologie der Heinrich Heine Universität, Forschungszentrum Julich, Wilhelm Johnen Str, Julich, D 52426, Germany
    Biotechnol Lett 26:1739-44. 2004
  8. ncbi request reprint Overproduction and characterization of a recombinant D-amino acid oxidase from Arthrobacter protophormiae
    Birgit Geueke
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Centre Julich, 52426 Julich, Germany
    Appl Microbiol Biotechnol 74:1240-7. 2007
  9. doi request reprint Highly efficient and stereoselective biosynthesis of (2S,5S)-hexanediol with a dehydrogenase from Saccharomyces cerevisiae
    Marion Muller
    Institute of Molecular Enzyme Technology, Research Center Julich, 52426 Julich, Germany
    Org Biomol Chem 8:1540-50. 2010
  10. ncbi request reprint Enzyme-catalyzed regio- and enantioselective ketone reductions
    Michael Muller
    Forschungszentrum Julich GmbH, 52425 Julich, Germany
    Adv Biochem Eng Biotechnol 92:261-87. 2005

Collaborators

  • Martina Pohl
  • Stephanie Bringer
  • Andreas Liese
  • Michael Muller
  • Christian Wandrey
  • K Niefind
  • Karl Erich Jaeger
  • Thorsten Eggert
  • Harald Groger
  • Andrea Weckbecker
  • Dalia Bulut
  • Birgit Geueke
  • Dietmar Schomburg
  • Julia Parkot
  • Michael Wolberg
  • Annette Faust
  • Kirsten Schroer
  • Thomas Drepper
  • Thomas Daussmann
  • Nils Helge Schlieben
  • Mutlu Kuzu
  • Karlheinz Drauz
  • Claudia Rollmann
  • Clara Ferloni
  • Nongnaphat Duangdee
  • Albrecht Berkessel
  • Murillo Villela Filho
  • Ralf Feldmann
  • Silke Bode
  • Petra Geilenkirchen
  • Rupert Pfaller
  • Stephanie Bringer-Meyer
  • Ursula Mackfeld
  • Stephan Lutz
  • Ivy Ai Wei Tan
  • Florian Heuser
  • Oliver May
  • Nicolas Orologas
  • Frank Rosenau
  • Susanne Wilhelm
  • Christian Leggewie
  • Francoise Chamouleau
  • Jörg Müller
  • Bettina Riebel
  • Jochen Buchs
  • Matthias Heinemann
  • Hendrik Hüsken
  • Tien Van Nguyen
  • Kofi Abokitse
  • Stefan Buchholz

Detail Information

Publications22

  1. ncbi request reprint Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis
    Werner Hummel
    Institut für Enzymtechnologie der Heinrich Heine Universität, Forschungszentrum Julich, Wilhelm Johnen Str, D 52426 Jülich, Germany
    Biotechnol Lett 25:51-4. 2003
    ..Highest activity was from pH 5.5-7 and at 40 degrees C. The enzyme requires dithiothreitol to prevent oxidative deactivation. The Km value for NADH was 24 microM...
  2. doi request reprint Strategies for regeneration of nicotinamide coenzymes emphasizing self-sufficient closed-loop recycling systems
    Werner Hummel
    Institute of Molecular Enzyme Technology at the Heinrich Heine University of Düsseldorf, Research Centre Julich, Stetternicher Forst, 52426 Julich, Germany Electronic address
    J Biotechnol 191:22-31. 2014
    ..This elegant method is applicable in special cases only but increasing numbers of examples have been published during the last years. ..
  3. ncbi request reprint An efficient and selective enzymatic oxidation system for the synthesis of enantiomerically pure D-tert-leucine
    Werner Hummel
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, im Forschungszentrum Jülich, 52426 Julich, Germany
    Org Lett 5:3649-50. 2003
    ..The l-amino acid was oxidized completely due to coupling of the primary reaction with a highly efficient irreversible NAD(+)-regenerating step by NADH oxidase...
  4. doi request reprint Purification, cloning, and overexpression of an alcohol dehydrogenase from Nocardia globerula reducing aliphatic ketones and bulky ketoesters
    Julia Parkot
    Institut für Molekulare Enzymtechnologie, Heinrich Heine Universitat Dusseldorf, Forschungzentrum Jülich, Stetternicher Forst, 52426, Julich, Germany
    Appl Microbiol Biotechnol 86:1813-20. 2010
    ....
  5. doi request reprint Regeneration of nicotinamide coenzymes: principles and applications for the synthesis of chiral compounds
    Andrea Weckbecker
    Institute of Molecular Enzyme Technology, Heinrich Heine University of Dusseldorf, Research Centre Julich, Stetternicher Forst, 52426, Julich, Germany
    Adv Biochem Eng Biotechnol 120:195-242. 2010
    ..An increasing number of examples in technical scale applications are known where nicotinamide dependent enzymes were used together with cofactor regenerating enzymes...
  6. pmc Crystallization and preliminary crystallographic analysis of a flavoprotein NADH oxidase from Lactobacillus brevis
    Mutlu Kuzu
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Centre Julich, 52426 Julich, Germany
    Acta Crystallogr Sect F Struct Biol Cryst Commun 61:528-30. 2005
    ..8, b = 95.7, c = 116.9 A, alpha = gamma = 90, beta = 103.8 degrees. The current diffraction limit is 4.0 A. The self-rotation function of the native data set is consistent with a NOX tetramer in the asymmetric unit...
  7. ncbi request reprint Improved synthesis of chiral alcohols with Escherichia coli cells co-expressing pyridine nucleotide transhydrogenase, NADP+-dependent alcohol dehydrogenase and NAD+-dependent formate dehydrogenase
    Andrea Weckbecker
    Institut für Molekulare Enzymtechnologie der Heinrich Heine Universität, Forschungszentrum Julich, Wilhelm Johnen Str, Julich, D 52426, Germany
    Biotechnol Lett 26:1739-44. 2004
    ..Cells that were permeabilized with toluene showed ketone reduction only if both cofactors were present...
  8. ncbi request reprint Overproduction and characterization of a recombinant D-amino acid oxidase from Arthrobacter protophormiae
    Birgit Geueke
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Centre Julich, 52426 Julich, Germany
    Appl Microbiol Biotechnol 74:1240-7. 2007
    ..Mainly, basic and hydrophobic D-amino acids were oxidized by the strictly enantioselective enzyme. After a high cell density fermentation, 2.29 x 10(6) U of D-AAO were obtained from 15 l of fermentation broth...
  9. doi request reprint Highly efficient and stereoselective biosynthesis of (2S,5S)-hexanediol with a dehydrogenase from Saccharomyces cerevisiae
    Marion Muller
    Institute of Molecular Enzyme Technology, Research Center Julich, 52426 Julich, Germany
    Org Biomol Chem 8:1540-50. 2010
    ..Furthermore, the enzyme's ability to reduce other keto-compounds, including further diketones, was studied, revealing that the application can be extended to alpha-diketones and aldehydes...
  10. ncbi request reprint Enzyme-catalyzed regio- and enantioselective ketone reductions
    Michael Muller
    Forschungszentrum Julich GmbH, 52425 Julich, Germany
    Adv Biochem Eng Biotechnol 92:261-87. 2005
    ..The obtained highly functionalized enantiopure alcohols are synthetically flexible chiral building blocks that offer new synthetic strategies for target- and diversity-oriented synthesis...
  11. ncbi request reprint Continuous asymmetric ketone reduction processes with recombinant Escherichia coli
    Kirsten Schroer
    Institut für Biotechnologie 2, Forschungszentrum Julich, 52425 Julich, Germany
    J Biotechnol 132:438-44. 2007
    ..5 and 2.8 mol L(-1), respectively. Even under these extreme conditions, the applied biocatalyst showed a good stability with only marginal leakage of intracellular cofactors...
  12. doi request reprint Screening, Molecular Cloning, and Biochemical Characterization of an Alcohol Dehydrogenase from Pichia pastoris Useful for the Kinetic Resolution of a Racemic β-Hydroxy-β-trifluoromethyl Ketone
    Dalia Bulut
    Institute of Molecular Enzyme Technology, Heinrich Heine University of Dusseldorf, Research Centre Julich, Wilhelm Johnen Strasse, 52426, Julich, Germany
    Chembiochem 17:1349-58. 2016
    ..PPADH shows a substrate preference for the reduction of linear and branched aliphatic aldehydes. Surprisingly, the enzyme shows no comparable activity towards ketones other than the β-hydroxy-β-trifluoromethyl ketone. ..
  13. ncbi request reprint Heterologous expression of Rhodococcus opacus L-amino acid oxidase in Streptomyces lividans
    Birgit Geueke
    Research Centre Julich, Institute of Enzyme Technology, Heinrich Heine University Dusseldorf, 52426 Julich, Germany
    Protein Expr Purif 28:303-9. 2003
    ..05 Umg(-1) was reached. Both the wild type and the recombinant L-AAO were purified to homogeneity. The expression systems described here now allow the structural and biochemical analysis of the L-AAO using genetic engineering methods...
  14. doi request reprint Development of a growth-dependent selection system for identification of L-threonine aldolases
    Dalia Bulut
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Centre Julich, Wilhelm Johnen Straße, 52426, Julich, Germany
    Appl Microbiol Biotechnol 99:5875-83. 2015
    ..In summary, it can be stated that a powerful screening tool was developed to identify easily by growth new L-specific threonine aldolases or other enzymes from genomic or metagenomic libraries liberating benzaldehyde. ..
  15. doi request reprint Chemoenzymatic synthesis of the chiral side-chain of statins: application of an alcohol dehydrogenase catalysed ketone reduction on a large scale
    Michael Wolberg
    Institute of Biotechnology 2, Research Center Julich, 52425 Julich, Germany
    Bioprocess Biosyst Eng 31:183-91. 2008
    ..Furthermore, studies directed towards improving the co-catalyst [NADP(H)] consumption of the enzymatic key step by kinetic studies and application of a biphasic reaction medium were performed...
  16. ncbi request reprint Practical asymmetric enzymatic reduction through discovery of a dehydrogenase-compatible biphasic reaction media
    Harald Groger
    Degussa AG, Project House Biotechnology, P O Box 1345, 63403 Hanau, Germany
    Org Lett 5:173-6. 2003
    ..The reductions with poorly water-soluble ketones were carried out at substrate concentrations of 10-200 mM, and the optically active (S)-alcohols were formed with moderate to good conversions and with up to >99% ee...
  17. ncbi request reprint Enantioselective reduction of ketones with "designer cells" at high substrate concentrations: highly efficient access to functionalized optically active alcohols
    Harald Groger
    Degussa AG, Service Center Biocatalysis, P O Box 1345, 63403 Hanau, Germany
    Angew Chem Int Ed Engl 45:5677-81. 2006
  18. ncbi request reprint Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity
    Nils Helge Schlieben
    Universitat zu Koln, Institut fur Biochemie, Zulpicher Strasse 47, D 50674 Köln, Germany
    J Mol Biol 349:801-13. 2005
    ..Moreover, it affects an extended proton relay system that has been identified recently as a critical element for the catalytic mechanism in SDR enzymes...
  19. ncbi request reprint Optimization of enzymatic gas-phase reactions by increasing the long-term stability of the catalyst
    Clara Ferloni
    Biochemical Engineering, RWTH Aachen University, 52056 Aachen, Germany
    Biotechnol Prog 20:975-8. 2004
    ..The stabilized catalyst preparation was employed in a continuous gas-phase reactor at different temperatures (25-60 degrees C). At 50 degrees C, a space-time yield of 107 g/L/d was achieved within the first 80 h of continuous reaction...
  20. ncbi request reprint The crystal structure of R-specific alcohol dehydrogenase from Lactobacillus brevis suggests the structural basis of its metal dependency
    Karsten Niefind
    Universitat zu Koln, Institut fur Biochemie, Zulpicher Strasse 47, Germany
    J Mol Biol 327:317-28. 2003
    ..Therefore, the presented structure of apo-RADH provides plausible explanations for the metal dependence of the enzyme...
  21. ncbi request reprint The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation
    Annette Faust
    Universitat zu Koln, Institut fur Biochemie, Zulpicher Strasse 47, D 50674 Köln, Germany
    J Mol Biol 367:234-48. 2007
    ..These results are of general relevance for the mechanism of flavoproteins and lead to the proposal of a common dehydrogenation step in the mechanism for l and d-amino acid oxidases...
  22. ncbi request reprint Novel biocatalysts for white biotechnology
    Thomas Drepper
    Institute of Molecular Enzyme Technology, Heinrich Heine University Dusseldorf, Research Center Julich, Julich, Germany
    Biotechnol J 1:777-86. 2006
    ..Furthermore, we have isolated and characterized biocatalysts relevant for the preparation of enantiopure compounds...