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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 Trimethylaminuria. Additionally we are shipping FMO1 Antibodies (18) and FMO1 Kits (7) and many more products for this protein.
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Data indicate that in contrast to FMO2 (show FMO2 Proteins) and FMO4 (show FMO4 Proteins), FMO1 is highly expressed in metabolic tissues, including liver, kidney, white adipose tissue (WAT) and brown adipose tissue (BAT (show BAAT Proteins)).
Fmo1, 2, 3, 4 and 5 exhibit distinct cell-, tissue-, sex- and developmental stage-specific patterns of expression.
The functional activity of Fmo1 was determined.
Deletion of the mouse Fmo1 gene results in enhanced pharmacological behavioral responses to imipramine.
Report developmental regulation of hepatic FMO1 expression.
Study tested the genetic effects of three FMOs genes (FMO1, FMO3 (show FMO3 Proteins), and FMO6P) on nicotine dependence by performing targeted sequencing on 2,852 nicotine-dependent and nondependent smokers; identified significant association signals for gene FMO1 and FMO6P
data support the role of FMO3 (show FMO3 Proteins) in the N-oxidation of OLA and implicate for the first time the contribution of FMO1 and its functional *6 variant in OLA disposition
polymorphisms in FMO1 are significant risk factors in the development of nicotine dependence and that the mechanism may involve variation in nicotine pharmacology.
The results of this study suggested that the alteration of FMO gene expression is a consequence of the pathological environment linked to oxidative stress related to mutated SOD1 (show SOD1 Proteins).
FMO1 expression is restricted to the fetus; FMO1 suppression occurred within 3 d postpartum in a process tightly coupled to birth, but not gestational age.
data from transient expression assays in HepG2 cells suggested this SNP could account for a 2- to 3-fold loss of FMO1 promoter activity.
"...in fetal liver, where FMO1 predominates attaining expression levels of (about) 32% of expressed CYP3A4 (show CYP3A4 Proteins)." p. 574 "...recent examples indicate that FMOs play a prominent role in the metabolism ...of important drugs." p. 575
FMO1 was found to be down-regulated in human adult brain tissue.
Early studies described in this review document that FMO1 is the most abundant FMO enzyme in the human fetal liver, whereas FMO3 (show FMO3 Proteins) is essentially absent.
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 Trimethylaminuria. Three forms of the enzyme, FMO1 found in fetal liver, FMO2 found in adult liver, and FMO3 are encoded by genes clustered in the 1q23-q25 region. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in drugs, pesticides, and xenobiotics.
flavin containing monooxygenase 1
, dimethylaniline monooxygenase [N-oxide-forming] 1
, FMO 1
, dimethylaniline oxidase 1
, hepatic flavin-containing monooxygenase 1
, Flavin-containing monooxygenase 1
, Flavin-containing monooxygenase 1 (fetal liver)
, fetal hepatic flavin-containing monooxygenase 1
, flavin-containing monooxygenase 1
, hepatic flavin-containing monooxygenase (FMO)
, FMO 1A1
, FMO form 1