Characterization of a thermostable flavin-containing monooxygenase from Nitrincola lacisaponensis (NiFMO)
| Autor: | Elvira Romero, Andrea Mattevi, Gautier Bailleul, Simone Savino, Nikola Lončar, Filippo Fiorentini, Marco W. Fraaije |
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| Přispěvatelé: | Biotechnology |
| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular Oceanospirillaceae Indigo bioproduction Protein Conformation Flavoprotein OXYGEN ACTIVATION Gene Expression Flavin-containing monooxygenase medicine.disease_cause Crystallography X-Ray Applied Microbiology and Biotechnology INDIGO Substrate Specificity 03 medical and health sciences Enzyme Stability medicine Escherichia coli Monooxygenase 030304 developmental biology Thermostability chemistry.chemical_classification 0303 health sciences biology 030306 microbiology FAD Temperature General Medicine Protein engineering biology.organism_classification Recombinant Proteins Enzyme chemistry Biochemistry FLAVOPROTEIN MONOOXYGENASES biology.protein Oxygenases Bacteria Biotechnology |
| Zdroj: | Applied Microbiology and Biotechnology, 103(4), 1755-1764. SPRINGER Applied Microbiology and Biotechnology |
| ISSN: | 1432-0614 0175-7598 |
| Popis: | The flavin-containing monooxygenases (FMOs) play an important role in drug metabolism but they also have a high potential in industrial biotransformations. Among the hitherto characterized FMOs, there was no thermostable representative, while such biocatalyst would be valuable for FMO-based applications. Through a targeted genome mining approach, we have identified a gene encoding for a putative FMO from Nitrincola lacisaponensis, an alkaliphilic extremophile bacterium. Herein, we report the biochemical and structural characterization of this newly discovered bacterial FMO (NiFMO). NiFMO can be expressed as active and soluble enzyme at high level in Escherichia coli (90-100 mg/L of culture). NiFMO is relatively thermostable (melting temperature (Tm) of 51 °C), displays high organic solvent tolerance, and accepts a broad range of substrates. The crystal structure of NiFMO was solved at 1.8 Å resolution, which allows future structure-based enzyme engineering. Altogether, NiFMO represents an interesting newly discovered enzyme with the appropriate features to develop into an industrially applied biocatalyst. |
| Databáze: | OpenAIRE |
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