The involvement of glutamine synthetase/glutamate synthase in ammonia assimilation by Aspergillus nidulans.
Wild-type Aspergillus nidulans grew equally well on NH4Cl, KNO3 or glutamine as the only nitrogen source. NADP+-dependent glutamate dehydrogenase (EC 1.4.1.4) and glutamine synthetase (GS; EC 6.3.1.2) activities varied with the type and concentration of nitrogen source supplied. Glutamate synthase (GOGAT) activity (EC 1.4.7.1) was detected but it was almost unaffected by the type and concentration of nitrogen source supplied. Ion exchange chromatography showed that the GOGAT activity was due to a distinct enzyme. Azaserine, an inhibitor of the GOGAT reaction, reduced the glutamate pool by 60%, indicating that GOGAT is involved in ammonia assimilation by metabolizing the glutamine formed by GS.
D000596:Amino Acids / Q000378:metabolism; D000641:Ammonia / Q000378:metabolism*; D001233:Aspergillus nidulans / Q000187:drug effects / Q000201:enzymology*; D001377:Azaserine / Q000494:pharmacology; D005970:Glutamate Synthase / Q000378:metabolism*; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D000637:Transaminases / Q000378:metabolism*
D000596:Amino Acids; D000641:Ammonia; D001377:Azaserine; D005970:Glutamate Synthase; D000637:Transaminases; D005974:Glutamate-Ammonia Ligase