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 ]
Churakova E, Arends IWCE, Hollmann F Increasing the Productivity of Peroxidase-Catalyzed Oxyfunctionalization: A Case Study on the Potential of Two-Liquid-Phase Systems
ChemCatChem, 5: 565-568
[ 2013 ]
Hahn F, Ullrich R, Hofrichter M, Liers C Experimental approach to follow the spatiotemporal wood degradation in fungal microcosms
Biotechnol. J., 8: 127-132
[ 2013 ]
Karich A, Kluge M, Ullrich R, Hofrichter M Benzene oxygenation and oxidation by the peroxygenase of Agrocybe aegerita
AMB Express, 3: 5-13
[ 2013 ]
Kluge M, Ullrich R, Scheibner K, Hofrichter M Formation of naphthalene hydrates in the enzymatic conversion of 1,2-dihydronaphthalene by two fungal peroxygenases and subsequent naphthalene formation
J. Mol. Cat. B, doi: 10.1016/j.molcatb.2013.08.017
[ 2013 ]
Liers C, Aranda E, Strittmatter E, Piontek K, Plattner D, Zorn H, Ullrich R, Hofrichter M Phenol oxidation by DyP-type peroxidases in comparison to fungal and plant peroxidases
J. Mol. Cat. B, doi: 10.1016/j.molcatb.2013.09.025
[ 2013 ]
Liers C, Pecyna MJ, Kellner H, Worrich A, Zorn H, Steffen KT, Hofrichter M, Ullrich R Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases
Appl. Microbiol. Biotechnol., 97: 5839-5849
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