Optimized oxidoreductases for medium and large scale industrial biotransformations
CLOSE
Project Secretariat
Dr Marta Pérez-Boada
E-mail: MPBoada@cib.csic.es
Consejo Superior de Investigaciones Científicas (CSIC)
Biological Research Centre (CIB)
Calle Ramiro de Maeztu 9, E-28040 Madrid, Spain
Phone: 34 918373112
Fax: 34 915360432
Mobile: 34 650080476
CLOSE
Private area
User:


Password:

publications
Total records: 126
Pages:    1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21  

[ 2016 ] Kellner H, Pecyna MJ, Buchhaupt M, Ullrich R, Hofrichter M Draft Genome Sequence of the Chloroperoxidase-Producing Fungus Caldariomyces fumago Woronichin DSM1256 Genome Announc., 4
[ 2016 ] Kracher D, Scheiblbrandner S, Felice AKG, Breslmayr E, Preims M, Ludwicka K, Haltrich D, Eijsink VG, Ludwig R Extracellular electron transfer systems fuel cellulose oxidative degradation Science, 352: 1098-1101
[ 2016 ] Linde D, Cañellas M, Coscolín C, Davó-Siguero I, Romero A, Lucas F, Ruiz-Dueñas FJ, Guallar V, Martínez AT Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase: An experimental and computational study Catal. Sci. Technol., 6: 6277-6285
[ 2016 ] Lourenço A, Rencoret J, Chemetova C, Gominho J, Gutiérrez A, del Río JC, Pereira H Lignin Composition and Structure Differs between Xylem, Phloem and Phellem in Quercus suber L. Front. Plant Sci., 7: 1612
[ 2016 ] Lucas F, Babot ED, Cañellas M, del Río JC, Kalum L, Ullrich R, Hofrichter M, Guallar V, Martínez AT, Gutiérrez A Molecular determinants for selective C25-hydroxylation of vitamins D2 and D3 by fungal peroxygenases Catal. Sci. Technol., 6: 288-295
[ 2016 ] Martínez AT How to break down crystalline cellulose Science, 352: 1050-1051
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).

Download the article for free until July 5th on: https://authors.elsevier.com/a/1Z3YPw0NEPWp

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