Changes in the enzyme activities involved in nitrogen assimilation in Mycobacterium smegmatis under various growth conditions.
Glutamate dehydrogenase (aminating) and glutamine synthetase activities were assayed in Mycobacterium smegmatis following growth on various carbon and nitrogen sources. The activities (expressed as nmoles product formed/min/mg crude extract protein) of these two enzymes were higher in crude extracts from glucose-grown cells than in glycerol- or fructose-grown cells. In the presence of succinate, pyruvate, fumarate or acetate in the growth medium, both these enzyme activities were lower than those in citrate-grown cells. The glutamate dehydrogenase (GDH) activity was the same in asparagine and glutamine-grown cells. Ammonium chloride, alanine or glutamic acid, when used as nitrogen source, resulted in low GDH activity as compared to asparagine-grown cells. Glutamine synthetase activity was considerably lower (2-4 fold) when the cells were grown on alanine, glutamine, glutamic acid or ammonium chloride as the nitrogen source than those in asparagine-grown cells. Glutamate and ammonium chloride, when present in the growth medium, repressed both glutamate dehydrogenase and glutamine synthetase, though the degree of repression was small. The results suggest that only a weak transcriptional control operates for these enzyme activities in M. smegmatis.
D000409:Alanine; D000643:Ammonium Chloride; D001216:Asparagine; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D005971:Glutamates; D018698:Glutamic Acid; D005973:Glutamine; D009161:Mycobacterium / Q000201:enzymology* / Q000254:growth & development
D005971:Glutamates; D000643:Ammonium Chloride; D005973:Glutamine; D018698:Glutamic Acid; D001216:Asparagine; D005969:Glutamate Dehydrogenase; D005974:Glutamate-Ammonia Ligase; D000409:Alanine