Optimized oxidoreductases for medium and large scale industrial biotransformations
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E-mail: MPBoada@cib.csic.es
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publications
Total records: 126
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[ 2015 ] Viña-Gonzalez J, González-Pérez D, Ferreira P, Martínez AT, Alcalde M Focused directed evolution of aryl-alcohol oxidase in yeast using chimeric signal peptides Appl. Environ. Microbiol., 81: 6451-6462
[ 2015 ] Wang X, Ullrich R, Hofrichter M, Groves JT Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive Proc. Natl. Acad. Sci. USA, 112: 3686-3691
[ 2014 ] Barrasa JM, Blanco MN, Esteve-Raventós F, Altés A, Checa J, Martínez AT, Ruiz-Dueñas FJ Wood and humus decay strategies by white-rot basidiomycetes correlate with two different dye decolorization and enzyme secretion patterns on agar plates Fungal Gen. Biol., doi: 10.1016/j.fgb.2014.03.007
[ 2014 ] Camarero S, Martínez MJ, Martínez AT Understanding lignin biodegradation for the improved utilization of plant biomass in modern biorefineries Biofuels, Bioprod. Bioref., 8: 615-625
[ 2014 ] Carro J, Ferreira P, Rodríguez L, Prieto A, Serrano A, Balcells B, Ardá A, Jiménez-Barbero J, Gutiérrez A, Ullrich R, Hofrichter M, Martínez AT 5-Hydroxymethylfurfural conversion by fungal aryl-alcohol oxidase and unspecific peroxygenase FEBS J., 282: 3218-3229
[ 2014 ] Fernandez-Fueyo E, Acebes S, Ruiz-Dueñas FJ, Martínez MJ, Romero A, Medrano FJ, Guallar V, Martínez AT Structural implications of the C-terminal tail in the catalytic and stability properties of manganese peroxidases from ligninolytic fungi Acta Crystal. D, 70: 3253-3265
year2019
Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan
Linde D, Ayuso-Fernández I, Ruiz-Dueñas FJ, Martínez AT
Arch. Biochem. Biophys., 668: 23-28

Dye-decolorizing peroxidase (DyP) from Auricularia auricula-judae and versatile peroxidase (VP) from Pleurotus eryngii oxidize the three mononitrophenol isomers. Both enzymes have been overexpressed in Escherichia coli and in vitro activated. Despite their very different three-dimensional structures, the nitrophenol oxidation site is located at a solvent-exposed aromatic residue in both DyP (Trp377) and VP (Trp164), as revealed by liquid chromatography coupled to mass spectrometry and kinetic analyses of nitrophenol oxidation by the native enzymes and their tryptophan-less variants (the latter showing 10–60 fold lower catalytic efficiencies).

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Official webpage of indox [ 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 garcíarincón