Optimized oxidoreductases for medium and large scale industrial biotransformations
Total records:
126
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[ 2017 ]
Alcalde M When directed evolution met ancestral enzyme resurrection
Microbial Biotechnol., 10: 22-24
[ 2017 ]
Ayuso-Fernández I, Martínez AT, Ruiz-Dueñas FJ Experimental recreation of the evolution of lignin-degrading enzymes from the Jurassic to date
Biotechnol. Biofuels, 10: 67
[ 2017 ]
Carro J, Martínez A, Medina M, Martínez AT, Ferreira P Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase
Phys. Chem. Chem. Phys., 19: 28666-28675
[ 2017 ]
González-Pérez D, Alcalde M The making of versatile peroxidase by directed evolution
Biocatalysis and Biotransformation, doi: 10.1080/10242422.2017.1363190
[ 2017 ]
Gygli G, Lucas F, Guallar V, van Berkel WJ The ins and outs of vanillyl alcohol oxidase: Identification of ligand migration paths
PLoS Comput. Biol., 13
[ 2017 ]
Martínez AT, Ruiz-Dueñas FJ, Camarero S, Serrano A, Linde D, Lund H, Vind J, Tovborg M, Herold-Majumdar OM, Hofrichter M, Liers C, Ullrich R, Scheibner K, Sannia G, Piscitelli A, Sener ME, Kılıç S, van Berkel WJ, Guallar V, et al. Oxidoreductases on their way to industrial biotransformations
Biotechnol. Adv., 35: 815-831
year2016
Rational Enzyme Engineering Through Biophysical and Biochemical Modeling
Acebes S, Fernandez-Fueyo E, Monza E, Lucas F, Almendral D, Ruiz-Dueñas FJ, Lund H, Martínez AT, Guallar V
ACS-Catalysis, 6: 1624-1629
Due to its importance in the pharmaceutical industry, ligand dynamic simulations have experienced a great expansion. Using all-atom models and cutting-edge hardware, one can perform nonbiased ligand migration, active site search, and binding studies. In this Letter, we demonstrate (and validate by PCR mutagenesis) how these techniques, when combined with quantum mechanics, open new possibilities in enzyme engineering. We provide a complete analysis where (1) biophysical simulations produce ligand diffusion and (2) biochemical modeling samples the chemical event. Using such broad analysis, we engineer a highly stable peroxidase activating the enzyme for new substrate oxidation after rational mutation of two nonconserved surface residues. In particular, we create a new surface-binding site, quantitatively predicting the in vitro change in oxidation rate obtained by mutagenic PCR and achieving a comparable specificity constant to active peroxidases.
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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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