Optimized oxidoreductases for medium and large scale industrial biotransformations
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Dr Marta Pérez-Boada
E-mail: MPBoada@cib.csic.es
Consejo Superior de Investigaciones Científicas (CSIC)
Biological Research Centre (CIB)
Calle Ramiro de Maeztu 9, E-28040 Madrid, Spain
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publications
Total records: 119
Pages:   1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20  

[ 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 ] Martínez AT, Camarero S, Ruiz-Dueñas FJ, Martínez MJ Biological Lignin Degradation Lignin Valorization: Emerging Approaches. Ed. Gregg Beckham. RSC: 199-225
[ 2018 ] Ullrich R, Poraj-Kobielska M, Scholze S, Halbout C, Sandvoss M, Pecyna MJ, Scheibner K, Hofrichter M Side chain removal from corticosteroids by unspecific peroxygenase J. Inorg. Biochem., 183: 84-93
[ 2017 ] Acebes S, Ruiz-Dueñas FJ, Toubes M, Saez-Jimenez V, Pérez-Boada M, Lucas F, Martínez AT, Guallar V Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases J. Phys. Chem. B, 121: 3946-3954
[ 2017 ] Alcalde M When directed evolution met ancestral enzyme resurrection Microbial Biotechnol., 10: 22-24
year2017
The ins and outs of vanillyl alcohol oxidase: Identification of ligand migration paths
Gygli G, Lucas F, Guallar V, van Berkel WJ
PLoS Comput. Biol., 13

Vanillyl alcohol oxidase (VAO) is a homo-octameric flavoenzyme belonging to the VAO/PCMH family. Each VAO subunit consists of two domains, the FAD-binding and the cap domain. VAO catalyses, among other reactions, the two-step conversion of p-creosol (2-methoxy-4-methylphenol) to vanillin (4-hydroxy-3-methoxybenzaldehyde). To elucidate how different ligands enter and exit the secluded active site, Monte Carlo based simulations have been performed. One entry/exit path via the subunit interface and two additional exit paths have been identified for phenolic ligands, all leading to the si side of FAD. We argue that the entry/exit path is the most probable route for these ligands. A fourth path leading to the re side of FAD has been found for the co-ligands dioxygen and hydrogen peroxide. Based on binding energies and on the behaviour of ligands in these four paths, we propose a sequence of events for ligand and co-ligand migration during catalysis. We have also identified two residues, His466 and Tyr503, which could act as concierges of the active site for phenolic ligands, as well as two other residues, Tyr51 and Tyr408, which could act as a gateway to the re side of FAD for dioxygen. Most of the residues in the four paths are also present in VAO’s closest relatives, eugenol oxidase and p-cresol methylhydroxylase. Key path residues show movements in our simulations that correspond well to conformations observed in crystal structures of these enzymes. Preservation of other path residues can be linked to the electron acceptor specificity and oligomerisation state of the three enzymes. This study is the first comprehensive overview of ligand and co-ligand migration in a member of the VAO/PCMH family, and provides a proof of concept for the use of an unbiased method to sample this process.

Official webpage of indox [ 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