| Title: | Prospecting Biotechnologically-Relevant Monooxygenases from Cold Sediment Metagenomes: An In Silico Approach |
| Author(s): | Musumeci MA; Lozada M; Rial DV; Mac Cormack WP; Jansson JK; Sjoling S; Carroll J; Dionisi HM; |
| Address: | "Laboratorio de Microbiologia Ambiental, Centro para el Estudio de Sistemas Marinos, CONICET, Puerto Madryn, Chubut U9120ACD, Argentina. musumeci@cenpat-conicet.gob.ar. Laboratorio de Microbiologia Ambiental, Centro para el Estudio de Sistemas Marinos, CONICET, Puerto Madryn, Chubut U9120ACD, Argentina. lozada@cenpat-conicet.gob.ar. Area Biologia Molecular, Departamento de Ciencias Biologicas, Facultad de Ciencias Bioquimicas y Farmaceuticas, Universidad Nacional de Rosario, CONICET, Suipacha 531 S2002LRK Rosario, Argentina. drial@fbioyf.unr.edu.ar. Instituto Antartico Argentino, Ciudad Autonoma de Buenos Aires C1010AAZ, Argentina. wmac@ffyb.uba.ar. Instituto de Nanobiotecnologia (NANOBIOTEC), CONICET-Universidad de Buenos Aires, Ciudad Autonoma de Buenos Aires C1113AAD, Argentina. wmac@ffyb.uba.ar. Earth and Biological Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA 99352, USA. janet.jansson@pnnl.gov. School of Natural Sciences and Environmental Studies, Sodertorn University, 141 89 Huddinge, Sweden. sara.sjoling@sh.se. Akvaplan-niva, Fram-High North Research Centre for Climate and the Environment, NO-9296 Tromso, Norway. jolynn.carroll@akvaplan.niva.no. ARCEx-Research Centre for Arctic Petroleum Exploration, Department of Geosciences, UiT The Arctic University of Norway, N-9037 Tromso, Norway. jolynn.carroll@akvaplan.niva.no. Laboratorio de Microbiologia Ambiental, Centro para el Estudio de Sistemas Marinos, CONICET, Puerto Madryn, Chubut U9120ACD, Argentina. hdionisi@cenpat-conicet.gob.ar" |
| ISSN/ISBN: | 1660-3397 (Electronic) 1660-3397 (Linking) |
| Abstract: | "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" |
| Keywords: | Amino Acid Sequence Bacteria/genetics Biocatalysis Biotechnology/methods Cold Temperature Cytochrome P-450 Enzyme System/genetics Kinetics Metagenome/*genetics Mixed Function Oxygenases/*genetics Oxidation-Reduction Phylogeny Sequence Alignment Substrate; |
| Notes: | "MedlineMusumeci, Matias A Lozada, Mariana Rial, Daniela V Mac Cormack, Walter P Jansson, Janet K Sjoling, Sara Carroll, JoLynn Dionisi, Hebe M eng Switzerland 2017/04/12 Mar Drugs. 2017 Apr 9; 15(4):114. doi: 10.3390/md15040114" |
