Glutamate dehydrogenase (GDH), encoded by GLUD1 gene, is a homohexameric enzyme located in the mitochondrial matrix in mammals. Structurally, it is composed of 2 trimers of subunits. The bottom domain of each trimer makes extensive contacts with the subunits from the other trimer. The top domain contains the NAD-binding domain, a long protrusion antenna region and the catalytic active site. GDH enzyme catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate and ammonia using NAD+/NADH as coenzyme. It has been demonstrated that the GDH enzymatic activity is modulated by several allosteric modulators. For instance, GTP is a potent allosteric inhibitor preventing the product release whereas ADP is a potent allosteric activator facilitating product release.