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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 ...
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.
Hydrolysis of the amino group of glutamine yielding glutamate and ammonium. Catalyzing enzyme: glutaminase (EC 3.5.1.2) 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 ...
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 ...
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 ...
The end product of the glutaminase reaction, glutamate, is a strong inhibitor of the reaction. Changes in glutamate dehydrogenase, which converts glutamate to 2-oxoglutarate and thereby decreases intramitochondrial glutamate levels, are thereby an important regulatory mechanism of glutaminase activity.
glutamate dehydrogenase (an enzyme that can convert glutamate to α-Ketoglutarate and vice versa). lactate dehydrogenase (used to convert NADH back to NAD + in anaerobic glycolysis, and in the back reaction to produce NADH) pyruvate dehydrogenase (A common enzyme that feeds the TCA Cycle by converting pyruvate to acetyl CoA, using NAD +.
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+ ...
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