6HNS

Structure of Nitrincola lacisaponensis flavin-containing monooxygenase (FMO) in complex with FAD and NADP+

Summary for 6HNS

• Entry DOI: 10.2210/pdb6hns/pdb
• Descriptor: Small molecule metabolism, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• Functional Keywords: drug metabolism, monooxygenase, thermostability, indigo, flavoprotein
• Biological source: Nitrincola lacisaponensis
• Total number of polymer chains: 2
• Total formula weight: 108341.97

Authors

Fiorentini, F.,Mattevi, A. (deposition date: 2018-09-17, release date: 2019-01-02, Last modification date: 2024-01-24)

Primary citation

Loncar, N.,Fiorentini, F.,Bailleul, G.,Savino, S.,Romero, E.,Mattevi, A.,Fraaije, M.W.
Characterization of a thermostable flavin-containing monooxygenase from Nitrincola lacisaponensis (NiFMO).
Appl. Microbiol. Biotechnol., 103:1755-1764, 2019

PubMed Abstract: 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 (T) 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.

PubMed: 30607493
DOI: 10.1007/s00253-018-09579-w

Experimental method

X-RAY DIFFRACTION (1.84 Å)