Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2019 ]
Linde D, Ayuso-Fernández I, Ruiz-Dueñas FJ, Martínez AT Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan
Arch. Biochem. Biophys., 668: 23-28
[ 2019 ]
Serrano A, Sancho F, Viña-Gonzalez J, Carro J, Alcalde M, Guallar V, Martínez AT Switching the substrate preference of fungal aryl-alcohol oxidase: towards stereoselective oxidation of secondary benzyl alcohols
Catal. Sci. Technol., doi: 10.1039/C8CY02447B
[ 2019 ]
Viña-Gonzalez J, Jimenez-Lalana D, Sancho F, Serrano A, Martínez AT, Guallar V, Alcalde M Structure‐Guided Evolution of Aryl Alcohol Oxidase from Pleurotus eryngii for the Selective Oxidation of Secondary Benzyl Alcohols
Adv. Synth. Catal., 361: 2514-2525
[ 2018 ]
Carro J, Fernandez-Fueyo E, Fernández-Alonso C, Cañada J, Ullrich R, Hofrichter M, Alcalde M, Ferreira P, Martínez AT Self-sustained enzymatic cascade for the production of 2,5-furandicarboxylic acid from 5-methoxymethylfurfural
Biotechnol. Biofuels, 11: 86-96
[ 2018 ]
Carro J, Ferreira P, Martínez AT, Gadda G Stepwise Hydrogen Atom and Proton Transfers in Dioxygen Reduction by Aryl-Alcohol Oxidase
Biochemistry, doi: 10.1021/acs.biochem.8b00106
[ 2018 ]
Ewing TA, Kühn J, Segarra S, Tortajada M, Zuhse R, van Berkel WJ Multigram Scale Enzymatic Synthesis of (R)‐1‐(4′‐Hydroxyphenyl)ethanol Using Vanillyl Alcohol Oxidase
Adv. Synth. Catal., 360: 2370-2376
year2017
Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
Acebes S, Ruiz-Dueñas FJ, Toubes M, Saez-Jimenez V, Pérez-Boada M, Lucas F, Martínez AT, Guallar V
J. Phys. Chem. B, 121: 3946-3954
Combining a computational analysis with site-directed mutagenesis, we have studied the long-range electron transfer pathway in versatile and lignin peroxidases, two enzymes of biotechnological interest that play a key role for fungal degradation of the bulky lignin molecule in plant biomass. The in silico study established two possible electron transfer routes starting at the surface tryptophan residue previously identified as responsible for oxidation of the bulky lignin polymer. Moreover, in both enzymes, a second buried tryptophan residue appears as a top electron transfer carrier, indicating the prevalence of one pathway. Site-directed mutagenesis of versatile peroxidase (from Pleurotus eryngii) allowed us to corroborate the computational analysis and the role played by the buried tryptophan (Trp244) and a neighbor phenylalanine residue (Phe198), together with the surface tryptophan, in the electron transfer. These three aromatic residues are highly conserved in all the sequences analyzed (up to a total of 169). The importance of the surface (Trp171) and buried (Trp251) tryptophan residues in lignin peroxidase has been also confirmed by directed mutagenesis of the Phanerochaete chrysosporium enzyme. Overall, the combined procedure identifies analogous electron transfer pathways in the long-range oxidation mechanism for both ligninolytic peroxidases, constituting a good example of how computational analysis avoids making extensive trial-error mutagenic experiments.
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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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