Prospecting biotechnologically-relevant monooxygenases from cold sediment metagenomes: An in silico approach

• Published in: Marine Drugs
• Main Authors: Lozada, Mariana, Rial, Daniela Veronica, Mac Cormack, Walter Patricio, Jansson, Janet K., Sjöling, Sara, Carroll, JoLynn, Dionisi, Hebe Monica
• Format: Article in Journal/Newspaper
• Language: English
• Published: Molecular Diversity Preservation International
• Subjects: BACTERIAL CYTOCHROME P450; BAEYER-VILLIGER MONOOXYGENASES; BIOPROSPECTING BIOCATALYSTS; MOLECULAR MODELING; PHYLOGENETIC ANALYSIS; Otras Ciencias Biológicas; Ciencias Biológicas; CIENCIAS NATURALES Y EXACTAS; Arctic; Argentina; Argentino; Carroll; Noruega; Norway; Pacific; Rosario; Suecia; Dirección Nacional del Antártico; Instituto Antártico Argentino; Arctic University of Norway; UiT The Arctic University of Norway
• Online Access: http://hdl.handle.net/11336/39169

The goal of this work was to identify sequences encoding monooxygenase biocatalysts with novel features by in silico mining an assembled metagenomic dataset of polar and subpolar marine sediments. The targeted enzyme sequences were Baeyer-Villiger and bacterial cytochrome P450 monooxygenases (CYP153). These enzymes have wide-ranging applications, from the synthesis of steroids, antibiotics, mycotoxins and pheromones to the synthesis of monomers for polymerization and anticancer precursors, due to their extraordinary enantio-, regio-, and chemo-selectivity that are valuable features for organic synthesis. Phylogenetic analyses were used to select the most divergent sequences affiliated to these enzyme families among the 264 putative monooxygenases recovered from the ~14 million protein-coding sequences in the assembled metagenome dataset. Three-dimensional structure modeling and docking analysis suggested features useful in biotechnological applications in five metagenomic sequences, such as wide substrate range, novel substrate specificity or regioselectivity. Further analysis revealed structural features associated with psychrophilic enzymes, such as broader substrate accessibility, larger catalytic pockets or low domain interactions, suggesting that they could be applied in biooxidations at room or low temperatures, saving costs inherent to energy consumption. This work allowed the identification of putative enzyme candidates with promising features from metagenomes, providing a suitable starting point for further developments. Fil: Lozada, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; Argentina Fil: Rial, Daniela Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas Centro Científico Tecnológico - CONICET -Rosario. Instituto de Biologia Molecular y Celular de Rosario; Argentina Fil: Mac Cormack, Walter Patricio. Ministerio de Relaciones Exteriores, Comercio Interno y Culto. Dirección Nacional del Antártico. Instituto Antártico Argentino; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina Fil: Jansson, Janet K. Pacific Northwest National Laboratory; Estados Unidos Fil: Sjöling, Sara. Södertörn University; Suecia Fil: Carroll, JoLynn. Fram-High North Research Centre for Climate and the Environment; Noruega. UiT The Arctic University of Norway; Noruega Fil: Dionisi, Hebe Monica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Centro Nacional Patagónico. Centro para el Estudio de Sistemas Marinos; Argentina