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  2. Oxidative deamination - Wikipedia

    en.wikipedia.org/wiki/Oxidative_deamination

    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 monoamine oxidase, which catalyzes the deamination of monoamines via addition of oxygen ...

  3. Glutamate dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Glutamate_dehydrogenase

    In the brain, the NAD+/NADH ratio in brain mitochondria encourages oxidative deamination (i.e. glutamate to α-ketoglutarate and ammonia). [1] In bacteria, the ammonia is assimilated to amino acids via glutamate and aminotransferases. [2] In plants, the enzyme can work in either direction depending on environment and stress.

  4. Glutamate dehydrogenase 1 - Wikipedia

    en.wikipedia.org/wiki/Glutamate_dehydrogenase_1

    GLUD1 catalyses the oxidative deamination of Glu to 2-oxoglutarate and free NH 4 + using either NAD + or NADP + as a co-factor. The reaction occurs with the transfer of a hydride ion from Glu's Cα to NAD(P) +, thereby forming 2-iminoglutarate, which is hydrolyzed to 2-oxoglutarate and NH 4 +.

  5. Glutamic acid - Wikipedia

    en.wikipedia.org/wiki/Glutamic_acid

    Glutamate also plays an important role in the body's disposal of excess or waste nitrogen. Glutamate undergoes deamination, an oxidative reaction catalysed by glutamate dehydrogenase, [17] as follows: glutamate + H 2 O + NADP + → α-ketoglutarate + NADPH + NH 3 + H + Ammonia (as ammonium) is then excreted predominantly as urea, synthesised in ...

  6. Protein catabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_catabolism

    Oxidative deamination is the first step to breaking down the amino acids so that they can be converted to sugars. The process begins by removing the amino group of the amino acids. The amino group becomes ammonium as it is lost and later undergoes the urea cycle to become urea, in the liver. It is then released into the blood stream, where it ...

  7. GLUD2 - Wikipedia

    en.wikipedia.org/wiki/GLUD2

    2747 n/a Ensembl ENSG00000182890 ENSG00000288118 n/a UniProt P49448 n/a RefSeq (mRNA) NM_012084 n/a RefSeq (protein) NP_036216 n/a Location (UCSC) Chr X: 121.05 – 121.05 Mb n/a PubMed search n/a Wikidata View/Edit Human Glutamate dehydrogenase 2, mitochondrial, also known as GDH 2, is an enzyme that in humans is encoded by the GLUD2 gene. This dehydrogenase is one of the family of glutamate ...

  8. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    Deamination is the removal of an amino group from a molecule. [1] Enzymes that catalyse this reaction are called deaminases. 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.

  9. Deamidation - Wikipedia

    en.wikipedia.org/wiki/Deamidation

    Deamidation reaction of Asn-Gly (top right) to Asp-Gly (at left) or iso(Asp)-Gly (in green at bottom right) Deamidation is a chemical reaction in which an amide functional group in the side chain of the amino acids asparagine or glutamine is removed or converted to another functional group.