Depression of nitrate reductase in the presence of excess ammonium in a unicellular alga growing under conditions of phosphate limitation.
Chemostat cultures of the unicellular alga Cyanidium caldarium have shown that under conditions of phosphate limitation nitrate reductase is completely derepressed even in cells growing in a large excess of ammonium, but that it occurs mainly in a catalytically inactive form. It is hypothesized that phosphate limitation contributes to maintaining intracellular level of glutamine suitable to stimulate inactivation but not repression of nitrate reductase. It is not excluded that in addition to variations in the intracellular level of glutamine, there are other metabolic events of the cell by which repression and inactivation of nitrate reductase could be differently influenced.
D004789:Enzyme Activation / Q000187:drug effects; D004793:Enzyme Reactivators; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D005973:Glutamine / Q000494:pharmacology; D006358:Hot Temperature; D009565:Nitrate Reductases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010710:Phosphates / Q000494:pharmacology*; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology*; D000461:Rhodophyta / Q000201:enzymology*
D004793:Enzyme Reactivators; D010710:Phosphates; D000644:Quaternary Ammonium Compounds; D005973:Glutamine; D009565:Nitrate Reductases; D005974:Glutamate-Ammonia Ligase