Glutamate deamination by glutamate dehydrogenase plays a central role in amino acid catabolism in plants.

Glutamate is of central importance in plant N metabolism since the biosynthesis of all other amino acids requires this compound. Glutamate dehydrogenase (GDH; EC 1.4.1.2), which catalyzes in vitro reversible reductive amination of 2-oxoglutatre to form glutamate, is a key player in the metabolism of glutamate. While most previous studies have indicated that the oxidative deamination is the in vivo direction of the GDH reaction, its physiological role has remained ambiguous for decades. We have recently isolated mutants for the two known Arabidopsis GDH genes and created a gdh double mutant. Our recent work revealed an increased susceptibility of the gdh double mutant to dark-induced C starvation, the first phenotype associated with the loss of GDH activity in plants. Monitoring the amino acid breakdown during the dark treatment also suggested that the deamination of glutamate catalyzed by GDH is central to the catabolism of many other amino acids.