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Endogenous Roles of Mammalian Flavin-Containing Monooxygenases
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Enzymatically Produced Trimethylamine N-Oxide: Conserving It or Eliminating It

Department of Life Sciences and Systems Biology, University of Turin, Via Accademia Albertina 13, 10123 Turin, Italy
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Catalysts 2019, 9(12), 1028; https://doi.org/10.3390/catal9121028
Received: 20 November 2019 / Revised: 29 November 2019 / Accepted: 30 November 2019 / Published: 4 December 2019
(This article belongs to the Special Issue Flavin Monooxygenases)
Trimethylamine N-Oxide (TMAO) is the product of the monooxygenation reaction catalyzed by a drug-metabolizing enzyme, human flavin-containing monooxygenase 3 (hFMO3), and its animal orthologues. For several years, researchers have looked at TMAO and hFMO3 as two distinct molecules playing specific but separate roles, the former to defend saltwater animals from osmotic or hydrostatic stress and the latter to process xenobiotics in men. The presence of high levels of plasmatic TMAO in elasmobranchs and other animals was demonstrated a long time ago, whereas the actual physiological role of hFMO3 is still unknown because the enzyme has been mainly characterized for its ability to oxidize drugs. Recently TMAO was found to be related to several human health conditions such as atherosclerosis, cardiovascular, and renal diseases. This correlation poses a striking question of how other vertebrates (and invertebrates) can survive in the presence of very high TMAO concentrations (micromolar in humans, millimolar in marine mammals and several hundred millimolar in elasmobranchs). Therefore, it is important to address how TMAO, its precursors, and FMO catalytic activity are interconnected.
Keywords: flavoprotein; FMO; TMAO; protein folding; cardiovascular; osmolyte; monooxygenase; microbiome; enzyme catalysis; drug metabolism flavoprotein; FMO; TMAO; protein folding; cardiovascular; osmolyte; monooxygenase; microbiome; enzyme catalysis; drug metabolism
MDPI and ACS Style

Catucci, G.; Querio, G.; Sadeghi, S.J.; Gilardi, G.; Levi, R. Enzymatically Produced Trimethylamine N-Oxide: Conserving It or Eliminating It. Catalysts 2019, 9, 1028.

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