6HNS

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

6HNS の概要

• エントリーDOI: 10.2210/pdb6hns/pdb
• 分子名称: Small molecule metabolism, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: drug metabolism, monooxygenase, thermostability, indigo, flavoprotein
• 由来する生物種: Nitrincola lacisaponensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 108341.97

構造登録者

Fiorentini, F.,Mattevi, A. (登録日: 2018-09-17, 公開日: 2019-01-02, 最終更新日: 2024-01-24)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.84 Å)