Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Synthesis of glutamine synthetase (GS) in anaerobic batch cultures of Escherichia coli was repressed when excess NH4+ was available, but derepressed during growth with a poor nitrogen source. In wild-type bacteria there was only a weak inverse correlation between the activities of GS and glutamate dehydrogenase (GDH) during growth in various media. No positive correlations were found between the activities of GS and nitrite reductase, or between GS and cytochrome c552: both of these proteins were synthesized normally by mutants that contained no active GS. Although activities of GS and GDH were low in two mutants that are unable to synthesize cytochrome c552 or reduce nitrite because of defects in the nirA gene, the nirA defect was separated from the GS and GDH defects by transduction with bacteriophage P1. Attempts to show that catabolite repression of proline oxidase synthesis could be relieved during NH4+ starvation also failed. It is, therefore, unlikely that nitrite reduction or proline oxidation by E. coli are under positive control by GS protein. The regulation of the synthesis of enzymes for the utilization of secondary nitrogen sources in E. coli, therefore, different from that in Klebsiella aerogenes, but is similar to that in Salmonella typhimurium.
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PMID:Lack of a regulatory function for glutamine synthetase protein in the synthesis of glutamate dehydrogenase and nitrite reductase in Escherichia coli K12. 1 79

Seventeen strains of the new species Bacillus azotoformans were isolated by enrichment culture in peptone broth inoculated with pasteurized soil and then incubated under N2O at 32 degrees C. The bacterium is a Gram-negative rod, motile with peritrichous flagella, which produces oval spores without exosporia in swollen sporangia. However, the cells have thick walls, mesosomes, and persistent septa characteristic of Gram-positive bacteria. The bacterium lacks fermentative activity, does not attack carbohydrates, has complex growth requirements, and will grow anaerobically only if one of the following electron acceptors is present: NO3-, NO2-, N2O, S4O6--, or fumarate. Nitrate, nitrite, and nitrous oxide are denitrified with the production of N2. The microorganism is mesophilic, gives a positive oxidase reaction, synthesizes a type c cytochrome, and does not hydrolyse gelatin, starch, or "Tween 80." Poly-beta-hydroxybutyric acid is snythesized when the bacterium is grown in a medium containing DL-3-hydroxybutyrate. The following enzymes are present: nitrate reductase A, respiratory nitrite reductase, tetrathionate and fumarate reductases, and L-glutamate dehydrogenase. The following enzymes are absent: thiosulfate reductase, urease, lecithinase, arginine dihydrolase, phenylalanine deaminase, and catalase. For the 17 strains, the mean value of the G = C percent of the DNA is 39.8 +/- 1.2. All the strains are highly similar.
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PMID:[Morphological, physiological and taxonomic studies of Bacillus azotoformans]. 65 12

The described bacterium was isolated by enrichment culture in peptone broth inoculated with garden soil, pasteurized and then put to incubate under N2O at 32 degrees. It is a Gram-negative rod, motile with peritrichous flagella, and producing oval spores without exosporium in swollen sporangia. However, cells have the thick walls, mesosomes and persistant septa characteristic of Gram-positive bacteria. It lacks fermentative activity, does not attack carbohydrates, has complex growth requirements, and will grow anaerobically only if one of the following electron acceptors is present: NO3, NO2, N2O, S4O6, and fumarate. Nitrate, nitrite, and nitrous oxide are denitrified with production of N2. The microorganism is mesophilic, gives a positive oxidase reaction, synthesizes a type of c cytochrome, and does not hydrolyse gelatin, starch nor "Tween 80". The following enzymes are present: nitrate reductase A, respiratory nitrite reductase, tetrathionate and fumarate reductases, L-glutamate dehydrogenase, and superoxide dismutase. The following enzymes are absent: thiosulfate reductase, urease, lecithinase, arginine dihydrolase, L-alanine dehydrogenase, phenylalanine desaminase, and catalase. The GC% of its DNA is 39. The bacterium described can be considered to be a new species. We propose the name Bacillus azotoformans n. sp.
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PMID:[A new, sporulating, denitrifying, mesophilic bacterium: Bacillus azotoformans N. SP. (author's transl)]. 102 Aug 72

A positive, genetic selection against the activity of the nitrogen regulatory (NTR) system was used to isolate insertion mutations affecting nitrogen regulation in Klebsiella aerogenes. Two classes of mutation were obtained: those affecting the NTR system itself and leading to the loss of almost all nitrogen regulation, and those affecting the nac locus and leading to a loss of nitrogen regulation of a family of nitrogen-regulated enzymes. The set of these nac-dependent enzymes included histidase, glutamate dehydrogenase, glutamate synthase, proline oxidase, and urease. The enzymes shown to be nac independent included glutamine synthetase, asparaginase, tryptophan permease, nitrate reductase, the product of the nifLA operon, and perhaps nitrite reductase. The expression of the nac gene was itself highly nitrogen regulated, and this regulation was mediated by the NTR system. The loss of nitrogen regulation was found in each of the four insertion mutants studied, showing that loss of nitrogen regulation resulted from the absence of nac function rather than from an altered form of the nac gene product. Thus we propose two classes of nitrogen-regulated operons: in class I, the NTR system directly activates expression of the operon; in class II, the NTR system activates nac expression and the product(s) of the nac locus activates expression of the operon.
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PMID:Role of the nac gene product in the nitrogen regulation of some NTR-regulated operons of Klebsiella aerogenes. 197 23

Freezing and thawing of Nitrosomonas, followed by centrifugation of the homogenate at 3,000 x g, resulted in a fraction which appeared to consist of an intact membrane-envelope complex and contained approximately 50% of the cell protein and more than 90% of the ubiquinone and cytochrome A-type mammalian cytochrome c oxidase activity. The supernatant fraction, resulting from subsequent centrifugation of the extract at 100,000 x g, contained approximately 50% of the cell protein and more than 80% of the B- and C-type cytochrome and P-463 and the enzymes glutamate dehydrogenase; hydroxylamine dehydrogenase; nitrite synthetase; nitrite reductase; and 2,6-dichlorophenolindophenol-, p-phenylenediamine-, pyrogallol-, and hydroquinone-oxidase. Data on the concentration of electron transport components in Nitrosomonas are presented.
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PMID:Electron transport systems of Nitrosomonas: isolation of a membrane-envelope fraction. 433 11

In L. minor grown in sterile culture, the primary enzymes of nitrate assimilation, nitrate reductase (NR), nitrite reductase (NiR) and glutamate dehydrogenase (GDH) change in response to nitrogen source. NR and NiR levels are low when grown on amino acids (hydrolyzed casein) or ammonia; both enzymes are rapidly induced on addition of nitrate, while addition of nitrite induces NiR only. Ammonia represses the nitrate induced synthesis of both NR and NiR.NADH dependent GDH activity is low when grown on amino acids and high when grown on nitrate or ammonia, but the activities of NADPH dependent GDH and Alanine dehydro-genase (AIDH) are much less affected by nitrogen source. NADH-GDH and AIDH are induced by ammonia, and it is suggested that these enzymes are involved in primary nitrogen assimilation.
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PMID:Nitrogen metabolis of Lemna minor. II. Enzymes of nitrate assimilation and some aspects of their regulation. 579 47

The metabolism of inorganic nitrogen compounds was studied in extracts of Penicillium atrovenetum which had been grown under conditions in which beta-nitropropionic acid (BNP) synthesis varied from 0 to 12.5 mumoles per ml. None of the extracts was able to oxidize ammonium ion or nitrite. An enzyme was detected which catalyzed the oxidation of hydroxylamine with cytochrome c as the electron acceptor. The activity of this enzyme was not related to the ability of the organism to produce BNP. Nitrate and nitrite reductase activities were detected only in P. atrovenetum cultures grown on nitrate as a nitrogen source. These results indicated that BNP synthesis is probably not directly associated with the metabolism of inorganic nitrogen compounds and that an organic pathway for the formation of the nitro group is more likely. The activities of certain enzymes related to the metabolism of aspartic acid were investigated. Aspartate ammonia-lyase activity could not be detected in P. atrovenetum extracts. Aspartate aminotransferase and glutamate dehydrogenase activities were found in the extracts but were highest in the cultures which did not produce BNP. beta-Nitroacrylic acid reductase activity was highest in extracts of cultures which were actively synthesizing BNP.
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PMID:Role of ammonium ion in the biosynthesis of beta-nitropropionic acid. 580 74

An important biochemical feature of autotrophs, land plants and algae, is their incorporation of inorganic nitrogen, nitrate and ammonium, into the carbon skeleton. Nitrate and ammonium are converted into glutamine and glutamate to produce organic nitrogen compounds, for example proteins and nucleic acids. Ammonium is not only a preferred nitrogen source but also a key metabolite, situated at the junction between carbon metabolism and nitrogen assimilation, because nitrogen compounds can choose an alternative pathway according to the stages of their growth and environmental conditions. The enzymes involved in the reactions are nitrate reductase (EC 1.6.6.1-2), nitrite reductase (EC 1.7.7.1), glutamine synthetase (EC 6.3.1.2), glutamate synthase (EC 1.4.1.13-14, 1.4.7.1), glutamate dehydrogenase (EC 1.4.1.2-4), aspartate aminotransferase (EC 2.6.1.1), asparagine synthase (EC 6.3.5.4), and phosphoenolpyruvate carboxylase (EC 4.1.1.31). Many of these enzymes exist in multiple forms in different subcellular compartments within different organs and tissues, and play sometimes overlapping and sometimes distinctive roles. Here, we summarize the biochemical characteristics and the physiological roles of these enzymes. We also analyse the molecular evolution of glutamine synthetase, glutamate synthase and glutamate dehydrogenase, and discuss the evolutionary relationships of these three enzymes.
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PMID:Nitrogen-assimilating enzymes in land plants and algae: phylogenic and physiological perspectives. 1220 56

In order to better understand the effects of heavy metals on the growth of plants, we decided to perform recovering experiments by following both chemical and physiological parameters in cadmium pre-stressed tomato seedlings after cadmium had been removed from the nutrient solution. The work shows that cadmium suppression results in resumption of growth activity. The biomass of leaves and stems rose steadily. The increase in root biomass exceeded those of leaves and stems. At the same time, nitrate content was increased to reach the level obtained with unstressed controls. In all the organs studied, the activities of the enzymes involved in the anabolic nitrogen primary assimilation pathways (nitrate reductase (NR), nitrite reductase (NiR) and glutamine synthetase (GS) soared after that cadmium had been removed. While NAD(+)-dependent glutamate dehydrogenase (GDH-NAD+) activity also rose progressively during the recovering time, the cognate NADH-dependent glutamate dehydrogenase (GDH-NADH) activity decreased. This result allows us to propose that the ammonia produced by the stress-induced protein catabolism is detoxified and re-assimilated by the GDH-NADH isoenzyme. On the basis of these results, we will discuss the ability of the plant to dilute the effects of pollutants during the recovering period. An important outcome of this work is that a transient contamination of the culture medium by pollutants is not necessarily followed by a significant depreciation in product yield or quality.
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PMID:[Reversibility of the effects of cadmium on the growth and nitrogen metabolism in the tomato(Lycopersicon esculentum)]. 1289 45

Tomato (Lycopersicon esculentum) seedlings were grown in the presence of cadmium. After 1 week of Cd treatment, a sharp decline in biomass accumulation in the leaves and roots was observed, together with a decrease in the rate of photosynthetic activity due to both Rubisco and chlorophyll degradation and stomata closure. Cadmium induced a significant decrease in nitrate content and inhibition of the activities of nitrate reductase, nitrite reductase, glutamine synthetase (GS) and ferredoxin-glutamate synthase. An increase in NADH-glutamate synthase and NADH-glutamate dehydrogenase activity was observed in parallel. The accumulation of ammonium into the tissues of treated plants was accompanied by a loss of total protein and the accumulation of amino acids. Gln represented the major amino acid transported through xylem sap of Cd-treated and control plants. Cadmium treatment increased the total amino acid content in the phloem, maintaining Gln/Glu ratios. Western and Northern blot analysis of Cd-treated plants showed a decrease in chloroplastic GS protein and mRNA and an increase in cytosolic GS and glutamate dehydrogenase transcripts and proteins. An increase in asparagine synthetase mRNA was observed in roots, in parallel with a strong increase in asparagine. Taken together, these results suggest that the plant response to Cd stress involved newly induced enzymes dedicated to coordinated leaf nitrogen remobilization and root nitrogen storage.
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PMID:Cadmium toxicity induced changes in nitrogen management in Lycopersicon esculentum leading to a metabolic safeguard through an amino acid storage strategy. 1557 44


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