Evidence That Glutamate Dehydrogenase Plays a Role in the Oxidative Deamination of Glutamate in Seedlings of Zea mays

Abstract

In order to investigate the role of glutamate dehydrogenase we have compared the metabolism of [¹⁵N]glutamate in young seedlings of wild-type and a glutamate dehydrogenase-null mutant of Zea mays. The principal labelled products in roots of wild-type seedlings are the amide nitrogen of glutamine, glutamine-amino nitrogen and ammonium. The incorporation of label into glutamine-amide is markedly inhibited by methionine sulfoximine. In contrast, little or no labelling of glutamine-amide or ammonium occurs in roots of the GDH1-null mutant, the major labelled product is the amino group of asparagine. In shoots of the wild type, ¹⁵N is recovered in the amide of glutamine, ammonium, the amino group of asparagine and other amino acids. In mutant shoots, over 75% of the label is recovered in the asparagine-amino group and there is little labelling of glutamine-amide or ammonium. These major differences in glutamate metabolism of wild-type and mutant seedlings are consistent with glutamate dehydrogenase functioning in the direction of oxidative deamination and having a role in protein catabolism of germinating seeds.