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  

[ 2013 ] Miki Y, Pogni R, Acebes S, Lucas F, Fernandez-Fueyo E, Baratto MC, Fernández MI, de los Ríos V, Ruiz-Dueñas FJ, Sinicropi A, Basosi R, Hammel KE, Guallar V, Martínez AT Formation of a tyrosine adduct involved in lignin degradation by Trametopsis cervina lignin peroxidase: A novel peroxidase activation mechanism Biochem. J., 452: 575-584
[ 2013 ] Peter S, Karich A, Ullrich R, Gröbe G, Scheibner K, Hofrichter M Enzymatic one-pot conversion of cyclohexane into cyclohexanone: Comparison of four fungal peroxygenases J. Mol. Cat. B, doi: 10.1016/j.molcatb.2013.09.016
[ 2013 ] Peter S, Kinne M, Ullrich R, Kayser G, Hofrichter M Epoxidation of linear, branched and cyclic alkenes catalyzed by unspecific peroxygenase Enz. Microb. Technol., 52: 370-376
[ 2013 ] Pezzella C, Lettera V, Piscitelli A, Giardina P, Sannia G Transcriptional analysis of Pleurotus ostreatus laccase genes Appl. Microbiol. Biotechnol., 97: 705-717
[ 2013 ] Piontek K, Strittmatter E, Ullrich R, Gröbe G, Pecyna MJ, Kluge M, Scheibner K, Hofrichter M, Plattner D Structural Basis of Substrate Conversion in a New Aromatic Peroxygenase: P450 Functionality with Benefits J. Biol. Chem., 288: 34767-34776
[ 2013 ] Ruiz-Dueñas FJ, Lundell T, Floudas D, Nagy LG, Barrasa JM, Hibbett DS, Martínez AT Lignin-degrading peroxidases in Polyporales: an evolutionary survey based on 10 sequenced genomes Mycologia, 105: 1428-1444
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