title: The enzymes of the ammonia assimilation in Pseudomonas aeruginosa.
abstract: Glutamine synthetase from Pseudomonas aeruginosa is regulated by repression/derepression of enzyme synthesis and by adenylylation/deadenylylation control. High levels of deadenylylated biosynthetically active glutamine synthetase were observed in cultures growing with limiting amounts of nitrogen while synthesis of the enzyme was repressed and that present was adenylylated in cultures with excess nitrogen. NADP- and NAD-dependent glutamate dehydrogenase could be separated by column chromatography and showed molecular weights of 110,000 and 220,000, respectively. Synthesis of the NADP-dependent glutamate dehydrogenase is repressed under nitrogen limitation and by growth on glutamate. In contrast, NAD-dependent glutamate dehydrogenase is derepressed by glutamate. Glutamate synthase is repressed by glutamate but not by excess nitrogen.
mesh_terms: D000481:Allantoin / Q000378:metabolism; D000581:Amidohydrolases / Q000378:metabolism; D000641:Ammonia / Q000378:metabolism; D004790:Enzyme Induction; D004794:Enzyme Repression; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D005970:Glutamate Synthase / Q000378:metabolism*; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D009584:Nitrogen / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D000637:Transaminases / Q000378:metabolism*; D014510:Urease / Q000378:metabolism
chemical_list: D000481:Allantoin; D000641:Ammonia; D005970:Glutamate Synthase; D005969:Glutamate Dehydrogenase; D000637:Transaminases; D000581:Amidohydrolases; D014510:Urease; C019659:allantoinase; D005974:Glutamate-Ammonia Ligase; D009584:Nitrogen