Optimized oxidoreductases for medium and large scale industrial biotransformations
Total records:
126
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[ 2015 ]
Bormann S, Gomez Baraibar A, Ni Y, Holtmann D, Hollmann F Specific oxyfunctionalisations catalysed by peroxygenases: opportunities, challenges and solutions
Catal. Sci. Technol., 5: 2038-2052
[ 2015 ]
Büttner E, Ullrich R, Strittmatter E, Piontek K, Plattner D, Hofrichter M, Liers C Oxidation and nitration of mononitrophenols by a DyP-type peroxidase
Arch. Biochem. Biophys., 574: 86-92
[ 2015 ]
Fernandez-Fueyo E, Linde D, Almendral D, López-Lucendo MF, Ruiz-Dueñas FJ, Martínez AT Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II)
Appl. Microbiol. Biotechnol., doi: 10.1007/s00253-015-6665-3
[ 2015 ]
Fernandez-Fueyo E, van Wingerden M, Renirie R, Wever R, Ni Y, Holtmann D, Hollmann F Chemoenzymatic Halogenation of Phenols by using the Haloperoxidase from Curvularia inaequalis
ChemCatChem, doi: 10.1002/cctc.201500862
[ 2015 ]
Ferreira P, Carro J, Serrano A, Martínez AT A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes
Mycologia, 107: 1105-1119
[ 2015 ]
Ferreira P, Hernández-Ortega A, Lucas F, Carro J, Herguedas B, Borrelli K, Guallar V, Martínez AT, Medina M Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase
FEBS J., 282: 3091-3106
year2015
Insights into Laccase Engineering from Molecular Simulations: Toward a Binding-Focused Strategy
Monza E, Lucas F, Camarero S, Alejaldre LC, Martínez AT, Guallar V
J. Phys. Chem. Lett., 6: 1447-1453
Understanding the molecular determinants of enzyme performance is of primary importance for the rational design of ad hoc mutants. A novel approach, which combines efficient conformational sampling and quick reactivity scoring, is used here to shed light on how substrate oxidation was improved during the directed evolution experiment of a fungal laccase (from Pycnoporus cinnabarinus), an industrially relevant class of oxidoreductases. It is found that the enhanced activity of the evolved enzyme is mainly the result of substrate arrangement in the active site, with no important change in the redox potential of the T1 copper. Mutations at the active site shift the binding mode into a more buried substrate position and provide a more favorable electrostatic environment for substrate oxidation. As a consequence, engineering the binding event seems to be a viable way to in silico evolution of oxidoreductases.
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[ industrialoxidoreductases ]. Optimized oxidoreductases for medium and large scale industrial biotransformations. This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under Grant Agreement nº: FP7-KBBE-2013-7-613549. © indox 2013. Developed by
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