Optimized oxidoreductases for medium and large scale industrial biotransformations
Project Secretariat
Dr Marta Pérez-Boada
E-mail: MPBoada@cib.csic.esConsejo 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
Private area
publications
Pages:
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[ 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
year2013
Radical formation on a conserved tyrosine residue is crucial for DyP activity
Strittmatter E, Wachter S, Liers C, Ullrich R, Hofrichter M, Plattner D, Piontek K
Arch. Biochem. Biophys., 537: 161-167
Dye-decolorizing peroxidases (DyPs) are able to cleave bulky anthraquinone dyes. The recently published crystal structure of AauDyPI reveals that a direct oxidation in the distal heme cavity can be excluded for most DyP substrates. It is shown that a surface-exposed tyrosine residue acts as a substrate interaction site for bulky substrates. This amino acid is conserved in eucaryotic DyPs but is missing in the structurally related chlorite dismutases (Clds). Dye-decolorizing peroxidases of procaryotic origin equally possess a conserved tyrosine in the same region of the polypeptide albeit not at the homologous position.
Official webpage of 
[ 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
[ 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