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Glutamate Dehydrogenase (GDH; EC 1.4.1.2) catalyzes the reversible amination of α-ketoglutarate to glutamate, and the polymerization of nucleoside triphosphate(s) to RNA. But the natural role of the reversible amination reaction is the subject of an expanding conversation. The aim was to illuminate the natural role of GDH through its RNA synthetic activity. Stoichiometric combinations of mineral salts that targeted the GDH subunit compositions were applied to field-cultivated peanuts. GDH of seeds were made to synthesize RNA in the deamination and then in the amination direction. Free amino acids were analyzed by HPLC. Glutamate synthase (GOGAT) was assayed by photometry. Free amino acid yields in-creased from the control’s lowest (9.8 kg·ha–1) and amination-deamination ratio (0.05) through 12.0 - 23.0 kg·ha–1 in the K-, N+K+P+S-, Pi-, N+S-, S-treated peanuts with amination-deamination ratios between 0.6 and 10.0 until at the P+K-treated peanut which had the highest amino acid yield (52.4 kg·ha–1) and the highest amination-deamination ratio (61). The Km and Vmax values of GOGAT were within the normal range. Yields of free amino acids resulting from GDH aminating activity increased from <1.0 kg·ha–1 in the control, through 2.2 in the N+S-, 6.84 in the P+N-, 17.3 in the N-, to 42.6 kg·ha–1 in the P+K- treated peanut. These results show that the natural role of the GDH amination activity is to assimilate escalating multiples of the quantities of NH4+ ion as assimilated via the GS-GOGAT pathway. Peanut protein yields increased in parallel with GDH aminating activities and free amino acid yields such that the control peanut had the lowest protein (<26.0 kg·ha–1) and the yields increased exponentially (500 - 600 kg·ha–1) through the K-, P+S-, Pi-, N-treated to 910 kg·ha–1 in the P+K-treated peanut with the highest aminating activity of GDH. The ability of GDH aminating activity to escalate protein yields of food crops could be employed to address proteinenergy malnutrition syndrome of developing nations

Using the RNA synthetic activity of glutamate dehydrogenase to illuminate the natural role of the enzyme