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The flavin-containing monooxygenase (FMO) protein family specializes in the oxidation of xeno-substrates in order to facilitate the excretion of these compounds from living organisms. [1] These enzymes can oxidize a wide array of heteroatoms , particularly soft nucleophiles , such as amines , sulfides , and phosphites .
Flavin-containing monooxygenase 3 (FMO3), also known as dimethylaniline monooxygenase [N-oxide-forming] 3 and trimethylamine monooxygenase, is a flavoprotein enzyme (EC 1.14.13.148) that in humans is encoded by the FMO3 gene.
Dimethylaniline monooxygenase [N-oxide-forming] 2 is an enzyme that in humans is encoded by the FMO2 gene. [5] [6] [7]The flavin-containing monooxygenases are NADPH-dependent enzymes that catalyze the oxidation of many drugs and xenobiotics.
Dimethylaniline monooxygenase [N-oxide-forming] 1 is an enzyme that in humans is encoded by the FMO1 gene. [5]Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in humans resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome ...
Trimethylaminuria (TMAU), also known as fish odor syndrome or fish malodor syndrome, [1] is a rare metabolic disorder that causes a defect in the normal production of an enzyme named flavin-containing monooxygenase 3 (FMO3).
“An anti-inflammatory diet is the selection of foods that reduce the chronic inflammatory response, while at the same time providing the building blocks for use by anti-inflammatory pathways ...
Dimethylaniline monooxygenase [N-oxide-forming] 5 is an enzyme in humans encoded by the FMO5 gene. [5] [6] [7]Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in man resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome ...
Kynurenine 3-monooxygenase is a dimer containing asymmetric subunits [5] and has one FAD-binding domain as its prosthetic group. [3] Kynurenine 3-monooxygenase contains a linker region involved in substrate binding following a second strand of an antiparallel β-sheet, a six-stranded antiparallel β-sheet domain, and an α-helix at the carboxy-terminal. [5]
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