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  2. Trimethylaminuria - Wikipedia

    en.wikipedia.org/wiki/Trimethylaminuria

    Normally, the FMO3 enzyme converts fishy-smelling trimethylamine into trimethylamine N-oxide which has no odor. If the enzyme is missing or its activity is reduced because of a mutation in the FMO3 gene, trimethylamine is not broken down and instead builds up in the body. As the compound is released in a person's sweat, urine, and breath, it ...

  3. Flavin-containing monooxygenase 3 - Wikipedia

    en.wikipedia.org/wiki/Flavin-containing_mono...

    FMO3 is the primary enzyme in humans which catalyzes the N-oxidation of trimethylamine into trimethylamine N-oxide; [8] [10] FMO1 also does this, but to a much lesser extent than FMO3. [13] [14] Genetic deficiencies of the FMO3 enzyme cause primary trimethylaminuria, also known as "fish odor syndrome".

  4. Trimethylamine N-oxide reductase - Wikipedia

    en.wikipedia.org/wiki/Trimethylamine_N-oxide...

    The enzyme has been purified from E. coli and the photosynthetic bacteria Roseobacter denitrificans. [1] Trimethylamine oxide is found at high concentrations in the tissues of fish, and the bacterial reduction of this compound to foul-smelling trimethylamine is a major process in the spoilage of fish. [2]

  5. Trimethylamine - Wikipedia

    en.wikipedia.org/wiki/Trimethylamine

    It is a gas at room temperature but is usually sold as a 40% solution in water. It is also sold in pressurized gas cylinders. TMA protonates to give the trimethylammonium cation. Trimethylamine is a good nucleophile, and this reactivity underpins most of its applications. Trimethylamine is a Lewis base that forms adducts with a variety of Lewis ...

  6. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy. The amino group is removed from the amino acid and converted to ammonia.

  7. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    The formation of a peptide bond requires an input of energy. The two reacting molecules are the alpha amino group of one amino acid and the alpha carboxyl group of the other amino acids. A by-product of this bond formation is the release of water (the amino group donates a proton while the carboxyl group donates a hydroxyl). [2]

  8. Biogenic amine - Wikipedia

    en.wikipedia.org/wiki/Biogenic_amine

    Some lactic acid bacteria isolated from commercial bottled yoghurt have been shown to produce biogenic amines. They play an important role as source of nitrogen and precursor for the synthesis of hormones, alkaloids, nucleic acids, proteins, amines and food aroma components. However, food containing high amounts of biogenic amines may have ...

  9. Purine metabolism - Wikipedia

    en.wikipedia.org/wiki/Purine_metabolism

    A key regulatory step is the production of 5-phospho-α-D-ribosyl 1-pyrophosphate by ribose-phosphate diphosphokinase, which is activated by inorganic phosphate and inactivated by purine ribonucleotides. It is not the committed step to purine synthesis because PRPP is also used in pyrimidine synthesis and salvage pathways.