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
Structural Basis of Substrate Conversion in a New Aromatic Peroxygenase: P450 Functionality with Benefits
Piontek K, Strittmatter E, Ullrich R, Gröbe G, Pecyna MJ, Kluge M, Scheibner K, Hofrichter M, Plattner D
J. Biol. Chem., 288: 34767-34776
Aromatic peroxygenases (APOs) represent a unique oxidoreductase sub-subclass of heme proteins with peroxygenase and peroxidase activity and were thus recently assigned a distinct EC classification (EC 1.11.2.1). They catalyze, inter alia, oxyfunctionalization reactions of aromatic and aliphatic hydrocarbons with remarkable regio and stereoselectivities. Compared with cytochrome P450, APOs appear to be the choice enzymes for oxyfunctionalizations in organic synthesis due to their independence from a cellular environment and their greater chemical versatility. Here, the first two crystal structures of a heavily glycosylated fungal aromatic peroxygenase (AaeAPO) are described. They reveal different pH-dependent ligand-binding modes. We model the fitting of various substrates in AaeAPO, illustrating the way the enzyme oxygenates polycyclic aromatic hydrocarbons (PAHs). Spatial restrictions by a phenylalanine pentad in the active-site environment govern substrate specificity in AaeAPO.
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