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  2. Glutamate dehydrogenase - Wikipedia

    en.wikipedia.org/wiki/Glutamate_dehydrogenase

    Glutamate dehydrogenase (GLDH, GDH) is an enzyme observed in both prokaryotes and eukaryotic mitochondria. The aforementioned reaction also yields ammonia, which in eukaryotes is canonically processed as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase ...

  3. Glutamate dehydrogenase 1 - Wikipedia

    en.wikipedia.org/wiki/Glutamate_dehydrogenase_1

    GLUD1 (glutamate dehydrogenase 1) is a mitochondrial matrix enzyme, one of the family of glutamate dehydrogenases that are ubiquitous in life, with a key role in nitrogen and glutamate (Glu) metabolism and energy homeostasis. This dehydrogenase is expressed at high levels in liver, brain, pancreas and kidney, but not in muscle.

  4. Glutaminolysis - Wikipedia

    en.wikipedia.org/wiki/Glutaminolysis

    2. Glutamate can be excreted or can be further metabolized to α-ketoglutarate. For the conversion of glutamate to α-ketoglutarate three different reactions are possible: Catalyzing enzymes: glutamate dehydrogenase (GlDH), EC 1.4.1.2; glutamate pyruvate transaminase (GPT), also called alanine transaminase (ALT), EC 2.6.1.2

  5. 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 ...

  6. Transamination - Wikipedia

    en.wikipedia.org/wiki/Transamination

    The products usually are either alanine, aspartate or glutamate, since their corresponding alpha-keto acids are produced through metabolism of fuels. Being a major degradative aminoacid pathway, lysine, proline and threonine are the only three amino acids that do not always undergo transamination and rather use respective dehydrogenase.

  7. Glutamate dehydrogenase (NAD(P)+) - Wikipedia

    en.wikipedia.org/wiki/Glutamate_dehydrogenase...

    Glutamate dehydrogenase (NAD(P)+) (EC 1.4.1.3, glutamic dehydrogenase, glutamate dehydrogenase [NAD(P)+]) is an enzyme with systematic name L-glutamate:NAD(P)+ oxidoreductase (deaminating). [ 1 ] [ 2 ] [ 3 ] This enzyme catalyses the following chemical reaction

  8. Glutamate dehydrogenase (NADP+) - Wikipedia

    en.wikipedia.org/wiki/Glutamate_dehydrogenase...

    Glutamate dehydrogenase (NADP+) (EC 1.4.1.4, glutamic dehydrogenase, dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)), glutamic acid dehydrogenase, L-glutamate dehydrogenase, L-glutamic acid dehydrogenase, NAD(P)+-glutamate dehydrogenase, NAD(P)H-dependent glutamate dehydrogenase, glutamate dehydrogenase (NADP+)) is an enzyme with systematic name L-glutamate:NADP+ ...

  9. Fasciolosis - Wikipedia

    en.wikipedia.org/wiki/Fasciolosis

    Elevation of liver enzyme activities, such as glutamate dehydrogenase (GLDH), gamma-glutamyl transferase (GGT), and lactate dehydrogenase (LDH), is detected in subacute or chronic fasciolosis from 12 to 15 weeks after ingestion of metacercariae.