Optimized oxidoreductases for medium and large scale industrial biotransformations
Total records:
126
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[ 2015 ]
Hofrichter M, Kellner H, Pecyna MJ, Ullrich R Fungal unspecific peroxygenases: heme-thiolate proteins that combine peroxidase and cytochrome p450 properties
Adv. Exp. Med. Biol., 851: 341-368
[ 2015 ]
Kracher D, Zahma K, Schulz C, Sygmund C, Gorton L, Ludwig R Inter-domain electron transfer in cellobiose dehydrogenase: modulation by pH and divalent cations
FEBS J., doi: 10.1111/febs.13310
[ 2015 ]
Linde D, Pogni R, Cañellas M, Lucas F, Guallar V, Baratto MC, Sinicropi A, Saez-Jimenez V, Coscolín C, Romero A, Medrano FJ, Ruiz-Dueñas FJ, Martínez AT Catalytic surface radical in dye-decolorizing peroxidase: A computational, spectroscopic and site-directed mutagenesis study
Biochem. J., 466: 253-262
[ 2015 ]
Linde D, Ruiz-Dueñas FJ, Fernandez-Fueyo E, Guallar V, Hammel KE, Pogni R, Martínez AT Basidiomycete DyPs: Genomic diversity, structural-functional aspects, reaction mechanism and environmental significance
Arch. Biochem. Biophys., 574: 66-74
[ 2015 ]
Maté D, Alcalde M Laccase engineering: From rational design to directed evolution
Biotechnol. Adv., 33: 25-40
[ 2015 ]
Molina-Espeja P, Ma S, Maté D, Ludwig R, Alcalde M Tandem-yeast expression system for engineering and producing unspecific peroxygenase
Enz. Microb. Technol., 73: 29-33
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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