Abstract
Purified rat liver glutamine synthetase is sensitive to inhibition by glutamine and histidine when studied in a Mn 2+ assay system. If Mg 2+ is substituted for Mn 2+, no inhibition is seen. Both glutamine and histidine are more effective inhibitors when glutamate is limiting in concentration during assay. Alpha-ketoglutarate and citrate activate or inhibit catalytic activity depending on the concentration of divalent cation present during assay, and largely appear to regulate activity by binding the divalent cation required for activity. These results suggest that direct or indirect interaction of divalent cations with enzyme, substrates, inhibitors, and activators may be of major significance in the cellular regulation of rat liver glutamine synthetase.
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