Oxidative deamination

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Oxidative deamination is a form of deamination that generates α-keto acids and other oxidized products from amine-containing compounds, and occurs primarily in the liver.[1] Oxidative deamination is stereospecific, meaning it contains different stereoisomers as reactants and products; this process is either catalyzed by L or D- amino acid oxidase and L-amino acid oxidase is present only in the liver and kidney.[2] Oxidative deamination is an important step in the catabolism of amino acids, generating a more metabolizable form of the amino acid, and also generating ammonia as a toxic byproduct. The ammonia generated in this process can then be neutralized into urea via the urea cycle.

Much of the oxidative deamination occurring in cells involves the amino acid

α-ketoglutarate (α-KG) and ammonia. Glutamate can then be regenerated from α-KG via the action of transaminases or aminotransferase, which catalyze the transfer of an amino group from an amino acid to an α-keto acid. In this manner, an amino acid can transfer its amine group to glutamate, after which GDH can then liberate ammonia via oxidative deamination. This is a common pathway during amino acid catabolism.[3]

Another enzyme responsible for oxidative deamination is

epinephrine.[4] Monoamine oxidases are important drug targets, targeted by MAO inhibitors (MAOIs) such as selegiline
. Glutamate dehydrogenase play an important role in oxidative deamination.

References

  1. ^ LibreTexts, Chemistry (29 August 2020). "Stage II of Protein Catabolism". Chemistry LibreTexts. Retrieved 5 December 2020.
  2. ISBN 9780124166974.{{cite book}}: CS1 maint: multiple names: authors list (link
    )
  3. ^ "Amino Acid Catabolism: Nitrogen". Rensselaer Polytechnic Institute. Archived from the original on 29 June 2017. Retrieved 20 June 2017.
  4. PMID 15279562
    .

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