Assimilation of ammonia in Paracoccus denitrificans.
Two pathways serve for assimilation of ammonia in Paracoccus denitrificans. Glutamate dehydrogenase (NADP+) catalyzes the assimilation at a high NH4+ concentration. If nitrate serves as the nitrogen source, glutamate is synthesized by glutamate-ammonia ligase and glutamate synthase (NADPH). At a very low NH4+ concentration, all three enzymes are synthesized simultaneously. No direct relationship exists between glutamate dehydrogenase (NADP+) and glutamate-ammonia ligase in P. denitrificans, while the glutamate synthase (NADPH) activity changes in parallel with that of the latter enzyme. Ammonia does not influence the induction or repression of glutamate dehydrogenase (NADP+). The inner concentration of metabolites indicates a possible repression of glutamate dehydrogenase (NADP+) by the high concentration of glutamine or its metabolic products as in the case when NH4+ is formed by assimilative nitrate reduction. No direct effect of the intermediates of nitrate assimilation on the synthesis of glutamate dehydrogenase (NADP+) was observed.
Department of Biochemistry, Faculty of Science, Masaryk University, Brno, Czechoslovakia.
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Mikes
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Chválová
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Mátlová
D000641:Ammonia / Q000378:metabolism*; D005969:Glutamate Dehydrogenase / Q000378:metabolism; D005970:Glutamate Synthase / Q000378:metabolism; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism; D005971:Glutamates / Q000378:metabolism; D018698:Glutamic Acid; D005973:Glutamine / Q000378:metabolism; D009584:Nitrogen / Q000378:metabolism; D010231:Paracoccus denitrificans / Q000378:metabolism*
D005971:Glutamates; D005973:Glutamine; D018698:Glutamic Acid; D000641:Ammonia; D005970:Glutamate Synthase; D005969:Glutamate Dehydrogenase; D005974:Glutamate-Ammonia Ligase; D009584:Nitrogen