Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2014 ]
Levasseur A, Lomascolo A, Chabrol O, Ruiz-Dueñas FJ, [...] , Martínez AT, [...] , Record E The genome of the white-rot fungus Pycnoporus cinnabarinus: a basidiomycete model with a versatile arsenal for lignocellulosic biomass breakdown
BMC Genomics, 15: 486
[ 2014 ]
Linde D, Coscolín C, Liers C, Hofrichter M, Martínez AT, Ruiz-Dueñas FJ Heterologous expression and physicochemical characterization of a fungal dye-decolorizing peroxidase from Auricularia auricula-judae
Protein Expr. Purif., 103: 28-37
[ 2014 ]
Macellaro G, Baratto MC, Piscitelli A, Pezzella C, Fabrizi de Biani F, Palmese A, Piumi F, Record E, Basosi R, Sannia G Effective mutations in a high redox potential laccase from Pleurotus ostreatus
Appl. Microbiol. Biotechnol., doi: 10.1007/s00253-013-5491-8
[ 2014 ]
Macellaro G, Pezzella C, Cicatiello P, Sannia G, Piscitelli A Fungal Laccases Degradation of Endocrine Disrupting Compounds
BioMed Research International, doi: 10.1155/2014/614038
[ 2014 ]
Martínez AT, Ruiz-Dueñas FJ, Gutiérrez A, del Río JC, Alcalde M, Liers C, Ullrich R, Hofrichter M, Scheibner K, Kalum L, Vind J, Lund H Search, engineering, and applications of new oxidative biocatalysts
Biofuels, Bioprod. Bioref., 8: 819-835
[ 2014 ]
Molina-Espeja P, García-Ruiz E, González-Pérez D, Ullrich R, Hofrichter M, Alcalde M Directed evolution of Unspecific Peroxygenase from Agrocybe aegerita
Appl. Environ. Microbiol., 80: 3496-3507
year2013
Formation of a tyrosine adduct involved in lignin degradation by Trametopsis
cervina lignin peroxidase: A novel peroxidase activation mechanism
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
Biochem. J., 452: 575-584
Lignin peroxidase (LiP) from Trametopsis cervina has an exposed catalytic tyrosine (Tyr-181)instead of the conserved tryptophan of other lignin-degrading peroxidases. Pristine LiP showed alag period in veratryl alcohol (VA) oxidation. However, LiP after turnover with H2O2/VA (VA-LiP)lacked this lag, and H2O2-pretreated LiP (H2O2-LiP) was inactive. MS analyses revealed that VALiPincludes one VA molecule covalently bound to the side-chain of Tyr-181, whereas H2O2-LiPcontains hydroxylated Tyr-181. No adduct is formed by the Y171N variant. Molecular dockingshowed that VA binding is favored by sandwich π stacking with Tyr-181 and Phe-89. EPRspectroscopy after peroxide activation of the pretreated LiPs showed other protein radicals than thetyrosine radical found in pristine LiP, which were assigned to a tyrosine/VA adduct radical in VALiPand a dihydroxyphenyalanine radical in H2O2-LiP. Both radicals are able to oxidize large lowredox-potential substrates, but H2O2-LiP is unable to oxidize high redox-potential substrates.Transient-state kinetics showed that the tyrosine/VA adduct strongly promotes (>100-fold)substrate oxidation by compound II, the rate-limiting step in catalysis. The novel activationmechanism is involved in ligninolysis, as demonstrated using lignin model substrates. This is thefirst report on autocatalytic modification, resulting in functional alteration, among class-IIperoxidases.
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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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