TY - GEN A1 - Martinez, Angel T. A1 - Ruiz-Duenas, Francisco J. A1 - Camarero, Susana A1 - Serrano, Ana A1 - Linde, Dolores A1 - Lund, Henrik A1 - Vind, Jesper A1 - Tovborg, Morton A1 - Herold-Majumdar, Owik M. A1 - Hofrichter, Martin A1 - Liers, Christiane A1 - Ullrich, René A1 - Scheibner, Katrin A1 - Sannia, Giovanni A1 - Piscitelli, Alessandra A1 - Sener, Mehmet E. A1 - Kilic, Sibel A1 - Berkel, Willem J. H. van A1 - Guallar, Víctor A1 - Lucas, Maria Fátima A1 - Zuhse, Ralf A1 - Ludwig, Roland A1 - Hollmann, Frank A1 - Fernández-Fueyo, Elena A1 - Record, Eric A1 - Faulds, Craig B. A1 - Tortajada, Marta A1 - Winckelmann, Ib A1 - Rasmussen, Jo-Anne A1 - Gelo-Pujic, Mirjana A1 - Gutiérrez, Ana A1 - Rio, José C. del A1 - Rencoret, Jorge A1 - Alcalde, Miguel T1 - Oxidoreductases on their way to industrial biotransformations T2 - Biotechnology Advances N2 - Fungi produce heme-containing peroxidases and peroxygenases, flavin-containing oxidases and dehydrogenases, and different copper-containing oxidoreductases involved in the biodegradation of lignin and other recalcitrant compounds. Heme peroxidases comprise the classical ligninolytic peroxidases and the new dye-decolorizing peroxidases, while heme peroxygenases belong to a still largely unexplored superfamily of heme-thiolate proteins. Nevertheless, basidiomycete unspecific peroxygenases have the highest biotechnological interest due to their ability to catalyze a variety of regio- and stereo-selective monooxygenation reactions with H2O2 as the source of oxygen and final electron acceptor. Flavo-oxidases are involved in both lignin and cellulose decay generating H2O2 that activates peroxidases and generates hydroxyl radical. The group of copper oxidoreductases also includes other H2O2 generating enzymes - copper-radical oxidases - together with classical laccases that are the oxidoreductases with the largest number of reported applications to date. However, the recently described lytic polysaccharide monooxygenases have attracted the highest attention among copper oxidoreductases, since they are capable of oxidatively breaking down crystalline cellulose, the disintegration of which is still a major bottleneck in lignocellulose biorefineries, along with lignin degradation. Interestingly, some flavin-containing dehydrogenases also play a key role in cellulose breakdown by directly/indirectly “fueling” electrons for polysaccharide monooxygenase activation. Many of the above oxidoreductases have been engineered, combining rational and computational design with directed evolution, to attain the selectivity, catalytic efficiency and stability properties required for their industrial utilization. Indeed, using ad hoc software and current computational capabilities, it is now possible to predict substrate access to the active site in biophysical simulations, and electron transfer efficiency in biochemical simulations, reducing in orders of magnitude the time of experimental work in oxidoreductase screening and engineering. What has been set out above is illustrated by a series of remarkable oxyfunctionalization and oxidation reactions developed in the frame of an intersectorial and multidisciplinary European RTD project. The optimized reactions include enzymatic synthesis of 1-naphthol, 25-hydroxyvitamin D3, drug metabolites, furandicarboxylic acid, indigo and other dyes, and conductive polyaniline, terminal oxygenation of alkanes, biomass delignification and lignin oxidation, among others. These successful case stories demonstrate the unexploited potential of oxidoreductases in medium and large-scale biotransformations. KW - Peroxygenase KW - Biotechnology Y1 - 2017 U6 - https://doi.org/10.1016/j.biotechadv.2017.06.003 SN - 1873-1899 SN - 0734-9750 VL - 35 IS - 6 SP - 815 EP - 831 ER - TY - GEN A1 - Lyu, Yu-Xuan A1 - Fu, Qiang A1 - Wilczok, Dominika A1 - Ying, Kejun A1 - King, Aaron A1 - Antebi, Adam A1 - Vojta, Aleksandar A1 - Stolzing, Alexandra A1 - Moskalev, Alexey A1 - Georgievskaya, Anastasia A1 - Maier, Andrea B. A1 - Olsen, Andrea A1 - Groth, Anja A1 - Simon, Anna Katharina A1 - Brunet, Anne A1 - Jamil, Aisyah A1 - Kulaga, Anton A1 - Bhatti, Asif A1 - Yaden, Benjamin A1 - Pedersen, Bente Klarlund A1 - Schumacher, Björn A1 - Djordjevic, Boris A1 - Kennedy, Brian A1 - Chen, Chieh A1 - Huang, Christine Yuan A1 - Correll, Christoph U. A1 - Murphy, Coleen T. A1 - Ewald, Collin Y. A1 - Chen, Danica A1 - Valenzano, Dario Riccardo A1 - Sołdacki, Dariusz A1 - Erritzoe, David A1 - Meyer, David A1 - Sinclair, David A. A1 - Chini, Eduardo Nunes A1 - Teeling, Emma C. A1 - Morgen, Eric A1 - Verdin, Eric A1 - Vernet, Erik A1 - Pinilla, Estefano A1 - Fang, Evandro F. A1 - Bischof, Evelyne A1 - Mercken, Evi M. A1 - Finger, Fabian A1 - Kuipers, Folkert A1 - Pun, Frank W. A1 - Gyülveszi, Gabor A1 - Civiletto, Gabriele A1 - Zmudze, Garri A1 - Blander, Gil A1 - Pincus, Harold A. A1 - McClure, Joshua A1 - Kirkland, James L. A1 - Peyer, James A1 - Justice, Jamie N. A1 - Vijg, Jan A1 - Gruhn, Jennifer R. A1 - McLaughlin, Jerry A1 - Mannick, Joan A1 - Passos, João A1 - Baur, Joseph A. A1 - Betts-LaCroix, Joe A1 - Sedivy, John M. A1 - Speakman, John R. A1 - Shlain, Jordan A1 - Maltzahn, Julia von A1 - Andreasson, Katrin I. A1 - Moody, Kelsey A1 - Palikaras, Konstantinos A1 - Fortney, Kristen A1 - Niedernhofer, Laura J. A1 - Rasmussen, Lene Juel A1 - Veenhoff, Liesbeth M. A1 - Melton, Lisa A1 - Ferrucci, Luigi A1 - Quarta, Marco A1 - Koval, Maria A1 - Marinova, Maria A1 - Hamalainen, Mark A1 - Unfried, Maximilian A1 - Ringel, Michael S. A1 - Filipovic, Milos A1 - Topors, Mourad A1 - Mitin, Natalia A1 - Roy, Nawal A1 - Pintar, Nika A1 - Barzilai, Nir A1 - Binetti, Paolo A1 - Singh, Parminder A1 - Kohlhaas, Paul A1 - Robbins, Paul D. A1 - Rubin, Paul A1 - Fedichev, Peter O. A1 - Kamya, Petrina A1 - Muñoz-Canoves, Pura A1 - de Cabo, Rafael A1 - Faragher, Richard G. A. A1 - Konrad, Rob A1 - Ripa, Roberto A1 - Mansukhani, Robin A1 - Büttner, Sabrina A1 - Wickström, Sara A. A1 - Brunemeier, Sebastian A1 - Jakimov, Sergey A1 - Luo, Shan A1 - Rosenzweig-Lipson, Sharon A1 - Tsai, Shih-Yin A1 - Dimmeler, Stefanie A1 - Rando, Thomas A. A1 - Peterson, Tim R. A1 - Woods, Tina A1 - Wyss-Coray, Tony A1 - Finkel, Toren A1 - Strauss, Tzipora A1 - Gladyshev, Vadim N. A1 - Longo, Valter D. A1 - Dwaraka, Varun B. A1 - Gorbunova, Vera A1 - Acosta-Rodríguez, Victoria A. A1 - Sorrentino, Vincenzo A1 - Sebastiano, Vittorio A1 - Li, Wenbin A1 - Suh, Yousin A1 - Zhavoronkov, Alex A1 - Scheibye-Knudsen, Morten A1 - Bakula, Daniela T1 - Longevity biotechnology: bridging AI, biomarkers, geroscience and clinical applications for healthy longevity T2 - Aging Y1 - 2024 U6 - https://doi.org/10.18632/aging.206135 SN - 1945-4589 VL - 16 IS - 20 SP - 12955 EP - 12976 PB - Impact Journals, LLC ER -