[3][4] Transgenic plants expressing microbial GLDHs are improved in tolerance to herbicide, water deficit, and pathogen infections.
GLDH is localised in mitochondria, therefore practically none is liberated in generalised inflammatory diseases of the liver such as viral hepatitides.
[citation needed] Enzyme immunoassay (EIA) for glutamate dehydrogenase (GDH) can be used as screening tool for patients with Clostridioides difficile infection.
[citation needed] In humans, the activity of glutamate dehydrogenase is controlled through ADP-ribosylation, a covalent modification carried out by the gene sirt4.
[citation needed] In microbes, the activity is controlled by the concentration of ammonium and or the like-sized rubidium ion, which binds to an allosteric site on GLDH and changes the Km (Michaelis constant) of the enzyme.
Bovine liver glutamate dehydrogenase was found to be regulated by nucleotides in the late 1950s and early 1960s by Carl Frieden.
[14] The activation of mammalian GDH by L-leucine and some other hydrophobic amino acids has also been long known,[15] however localization of the binding site was not clear.
[16] Mutations which alter the allosteric binding site of GTP cause permanent activation of glutamate dehydrogenase, and lead to hyperinsulinism-hyperammonemia syndrome.