Abstract
The effects of ATP and GTP on the activities of ox liver and brain glutamate dehydrogenase were determined in the absence and presence of added Mg2+ ions. Although GTP was an inhibitor of the enzyme reaction assayed in the direction of NAD+ reduction, the Mg complex of this nucleotide had no effect on the activity. Similarly, the Mg complex of ATP was without effect on the activity of the enzyme, although the free nucleotide was an activator. It apparently is important to take account of Mg complex formation when considering the regulatory actions of these nucleotides.