Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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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
First Crystal Structure of a Fungal High-Redox Potential Dye-decolorizing Peroxidase: Substrate Interaction Sites and Long-Range Electron Transfer
Strittmatter E, Liers C, Ullrich R, Wachter S, Hofrichter M, Plattner D, Piontek K
J. Biol. Chem., 288: 4095-4102
DyP-type peroxidases (DyP = dye decolorizing peroxidases) belong to the large group of heme peroxidases. They utilize hydrogen peroxide to catalyze oxidations of various organic compounds. AauDyPI from Auricularia auricula-judae (Fungi) was crystallized and its crystal structure was determined at 2.1 A resolution. The mostly helical structure also shows a beta-sheet motif typical for DyPs and Cld-related structures and includes the complete poypeptide chain. At the distal side of the heme molecule, a flexible aspartate residue (Asp168) plays a key role in catalysis. It guides incoming hydrogen peroxide toward the heme iron and mediates proton rearrangement in the process of Compound I formation. Afterwards, its side chain changes its conformation now pointing toward the protein backbone. We propose an extended functionality of Asp168, that acts like a gatekeeper by altering the width of the heme cavity access channel. Chemical modifications of potentially redox-active amino acids show that a tyrosine is involved in substrate interaction. Using spin trapping experiments a transient radical on the surface-exposed Tyr337 was identified as the oxidation site for bulky substrates. A possible long-range electron transfer (LRET) pathway from the surface of the enzyme to the redox cofactor (heme) is discussed.
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[ 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
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