Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Changes in the enzyme activities involved in nitrogen assimilation in Mycobacterium smegmatis under various growth conditions. 289 60

It was shown that NAD(P)(+)-dependent glutamate dehydrogenase from bovine liver (EC 1.4.1.3) was activated under the action of ammonium chloride in concentration which corresponded to the level of ammonium in normal blood (2-10 mM). Ammonium chloride increases the activity of glutamate dehydrogenase 1.8 times. Having enhanced the level of ammonium chloride to the amount which corresponds to the level of ammonium ions in blood during the pathology (10-25 mM), this substance inhibited the enzyme activity of glutamate dehydrogenase. Influence of 20 mM ammonium chloride on IR-spectra of NAD(P)(+)-dependent glutamate dehydrogenase in the deuterium oxide solution leads to the widening of the absorption line at 3300 cm-1 toward the higher energy. It is supposed that inhibition action of ammonium ions on the activity of glutamate dehydrogenase is connected with partial destruction of stereoregular hydrogen bonds in the enzyme molecule.
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PMID:[Effect of ammonium chloride on NDP(P)+-dependent glutamate dehydrogenase from bovine liver]. 950 71