Abstract
Evidence is presented showing that the NADPH-linked glutamic dehydrogenase (anabolic GDHase) plays a key role in the regulation of nitrogen catabolism. In a mutant lacking anabolic GDHase activity (ddh-A mutation) the sensitivity of the general amino acid permease to ammonia is strongly depressed and three other independent activities are also largely liberated from ammonia inhibition. Neither intracellular ammonia nor 2-oxoglutarate alone can be considered as effectors of this regulation, but NADPH, NADP, the enzyme itself, or combinations of different effectors were not eliminated.
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More From: Biochemical and Biophysical Research Communications
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