Effect of trophic conditions and humic acid on alanine transamination in wheat plants

In dialyzed extracts from winter wheat plants an intensive enzymatical transamination reaction occurred between L-α-alanine and α-ketoglutaric acid (L-α-alanine + + 2-oxoglutarate = pyruvate + L-glutamate, EC 2.6.1.2) as well as a weak nonenzymatical transamination reaction, practically immeasurable. Pyridoxal-5’-phosphate strongly affected the reaction rate. Besides the transamination product-glutamate, γ-aminobutyric acid was formed in this reaction. This amino acid could have originated neither via proteolysis of the enzyme extract, nor via decarboxylation from glutamate formed, nor via transamination of succinic-γ-semialdehyde after α-ketoglutarate decarboxylation. This was the only case of its formation in the transamination reactions investigated in our laboratory — it originated from the alanine-glutamate reaction only, and the mechanism of its biosynthesis cannot be elucidated for the present. Dialysates from shoots exhibited a significantly higher enzymatic activity in comparison with those from roots. The effect of trophic conditions (Knop’s nutrient solution, a water solution of potassium humate, water) was not revealed when calculating per dry weight unit. However, when calculating per protein unit an increased activity was found in the dialysates from shoots of both nutrient — deficient variants. Roots of plants cultivated in potassium humate had the lowest activity. The discussion concerns the possibility of an adaptive use of this transamination for increasing the essential glutamate level in green parts of the plants cultivated under unfavourable nutritive conditions, and also deals with a further characteristic of the differing metabolism of plants cultivated in humate.