glutamate dehydrogenase

The first rapid diagnostic tests were using P. falciparum glutamate dehydrogenase as antigen.

Based on which cofactor is used, glutamate dehydrogenase enzymes are divided into the following three classes:

Glutamate can be deaminated by glutamate dehydrogenase or transaminated to form α-ketoglutarate.

Glutamate dehydrogenase pseudogene 5, also known as GLUDP5, is a human gene.

Humans express the following glutamate dehydrogenase isozymes:

Glutamate dehydrogenase catalyzes the reductive amination of α-ketoglutarate to glutamate.

The ammonia produced in neurons is fixed into α-ketoglutarate by the glutamate dehydrogenase reaction to form glutamate.

There are several versions of the enzyme glutamate dehydrogenase (GDH) encoded in the genome.

Oxidative deamination of glutamate by glutamate dehydrogenase.

The difficulty of rooting the universal tree of life using protein trees is also emphasized by our recent analysis of glutamate dehydrogenase phylogeny.

He accomplished this considerable feat using mutants of Neurospora crassa deficient in a specific enzyme called glutamate dehydrogenase.

Ammonia incorporation in animals and microbes occurs through the actions of glutamate dehydrogenase and glutamine synthetase.

In humans, the activity of glutamate dehydrogenase is controlled through ADP-ribosylation, a covalent modification carried out by the gene sirt4.

Glutamate dehydrogenase 2 is localized to the mitochondrion and acts as a homohexamer to recycle glutamate during neurotransmission.

Glutamate undergoes deamination, an oxidative reaction catalysed by glutamate dehydrogenase, as follows:

Glutaminase is expressed in periportal hepatocytes, where it generates NH (ammonia) for urea synthesis, as does glutamate dehydrogenase.

Glutamate dehydrogenase provides an oxidizable carbon source used for the production of energy as well as a reduced electron carrier, NADH.

Hyperinsulin Hyperammonia syndrome (HIHA) due to Glutamate dehydrogenase 1 gene.

Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate.

The significant increase of GLDH (glutamate dehydrogenase) was recorded from 14 week after infection in goats experimentally infected with F. magna.

One NADH molecule is reduced by the enzyme glutamate dehydrogenase in the conversion of glutamate to ammonium and α-ketoglutarate.

Mutations alter the allostric binding site of GTP cause permanent activation of glutamate dehydrogenase lead to disorder known as hyperinsulinism-hyperammonemia.

This is the origin of GLUD2 , a retrogene derived from GLUD1 , which encodes glutamate dehydrogenase.

These allow GLUD2 -encoded glutamate dehydrogenase to work better in the brain than the GLUD1 -encoded enzyme.

Glutamate dehydrogenase (requires NADH or NADPH)