flavin-adenine-dinucleotide and trimethylamine

flavin-adenine-dinucleotide has been researched along with trimethylamine* in 2 studies

Other Studies

2 other study(ies) available for flavin-adenine-dinucleotide and trimethylamine

Article	Year
Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA. Genomics, 1997, Dec-01, Volume: 46, Issue:2 The inherited metabolic disorder trimethylaminuria (fish-odor syndrome) is associated with defective hepatic N-oxidation of dietary-derived trimethylamine catalyzed by flavin-containing monooxygenase (FMO). As FMO3 encodes the major form of FMO expressed in adult human liver, it represents the best candidate gene for the disorder. The structural organization of FMO3 was determined by sequencing the products of exon-to-exon and vectorette PCR, the latter through the use of vectorette libraries constructed directly from genomic DNA. The gene contains one noncoding and eight coding exons. Knowledge of the exon/intron organization of the human FMO3 gene enabled each of the coding exons of the gene, together with their associated flanking intron sequences, to be amplified from genomic DNA and will thus facilitate the identification of mutations in FMO3 in families affected with fish-odor syndrome. Topics: Exons; Flavin-Adenine Dinucleotide; Humans; Introns; Metabolism, Inborn Errors; Methylamines; Molecular Sequence Data; NADP; Odorants; Oxygenases; Polymerase Chain Reaction; Sequence Analysis, DNA	1997
The FAD-containing monooxygenase-catalyzed N-oxidation and demethylation of trimethylamine in rat liver microsomes. Drug metabolism and drug interactions, 1991, Volume: 9, Issue:3-4 Trimethylaminuria (TMAuria), the excessive urinary excretion of the odorous trimethylamine (TMA), accompanies elimination of TMA in sweat and corresponding "fish-odor" syndrome. TMA was oxidized in vitro in rat liver microsomes from male Sprague-Dawley rats to TMA N-oxide and N-demethylated to dimethylamine (DMA). Both reactions were inhibited to 1-3% of normal activity by preincubation of microsomes without NADPH-generating system at 37 degrees C for 10 minutes indicating the FAD-containing monooxygenase-catalyzed reactions. On the other hand, the reactions were not inhibited by gas phase containing up to 80% carbon monoxide/20% oxygen mixture. The results are compatible with the hypothesis that in rat liver microsomes the N-oxygenation and N-demethylation of TMA are catalyzed only or predominantly by FAD-containing monooxygenases, and the cytochrome P-450 monooxygenases play a negligible, if any, role. Topics: Animals; Chromatography, Gas; Cytochrome P-450 Enzyme System; Dealkylation; Flavin-Adenine Dinucleotide; In Vitro Techniques; Male; Methylamines; Microsomes, Liver; Mixed Function Oxygenases; NAD; NADP; Oxidation-Reduction; Rats; Rats, Inbred Strains	1991

Article

Year

Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA.

Genomics, 1997, Dec-01, Volume: 46, Issue:2

The inherited metabolic disorder trimethylaminuria (fish-odor syndrome) is associated with defective hepatic N-oxidation of dietary-derived trimethylamine catalyzed by flavin-containing monooxygenase (FMO). As FMO3 encodes the major form of FMO expressed in adult human liver, it represents the best candidate gene for the disorder. The structural organization of FMO3 was determined by sequencing the products of exon-to-exon and vectorette PCR, the latter through the use of vectorette libraries constructed directly from genomic DNA. The gene contains one noncoding and eight coding exons. Knowledge of the exon/intron organization of the human FMO3 gene enabled each of the coding exons of the gene, together with their associated flanking intron sequences, to be amplified from genomic DNA and will thus facilitate the identification of mutations in FMO3 in families affected with fish-odor syndrome.

Topics: Exons; Flavin-Adenine Dinucleotide; Humans; Introns; Metabolism, Inborn Errors; Methylamines; Molecular Sequence Data; NADP; Odorants; Oxygenases; Polymerase Chain Reaction; Sequence Analysis, DNA

1997

The FAD-containing monooxygenase-catalyzed N-oxidation and demethylation of trimethylamine in rat liver microsomes.

Drug metabolism and drug interactions, 1991, Volume: 9, Issue:3-4

Trimethylaminuria (TMAuria), the excessive urinary excretion of the odorous trimethylamine (TMA), accompanies elimination of TMA in sweat and corresponding "fish-odor" syndrome. TMA was oxidized in vitro in rat liver microsomes from male Sprague-Dawley rats to TMA N-oxide and N-demethylated to dimethylamine (DMA). Both reactions were inhibited to 1-3% of normal activity by preincubation of microsomes without NADPH-generating system at 37 degrees C for 10 minutes indicating the FAD-containing monooxygenase-catalyzed reactions. On the other hand, the reactions were not inhibited by gas phase containing up to 80% carbon monoxide/20% oxygen mixture. The results are compatible with the hypothesis that in rat liver microsomes the N-oxygenation and N-demethylation of TMA are catalyzed only or predominantly by FAD-containing monooxygenases, and the cytochrome P-450 monooxygenases play a negligible, if any, role.

Topics: Animals; Chromatography, Gas; Cytochrome P-450 Enzyme System; Dealkylation; Flavin-Adenine Dinucleotide; In Vitro Techniques; Male; Methylamines; Microsomes, Liver; Mixed Function Oxygenases; NAD; NADP; Oxidation-Reduction; Rats; Rats, Inbred Strains

1991