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PubMed2006

Enzymatic evidence for the key role of arginine in nitrogen translocation by arbuscular mycorrhizal fungi.

Key enzymes of the urea cycle and (15)N-labeling patterns of arginine (Arg) were measured to elucidate the involvement of Arg in nitrogen translocation by arbuscular mycorrhizal (AM) fungi. Mycorrhiza was established between transformed carrot (Daucus carota) roots and Glomus intraradices in two-compartment petri dishes and three ammonium levels were supplied to the compartment containing the extraradical mycelium (ERM), but no roots. Time courses of specific enzyme activity were obtained for glutamine synthetase, argininosuccinate synthetase, arginase, and urease in the ERM and AM roots. (15)NH(4)(+) was used to follow the dynamics of nitrogen incorporation into and turnover of Arg. Both the absence of external nitrogen and the presence of L-norvaline, an inhibitor of Arg synthesis, prevented the synthesis of Arg in the ERM and resulted in decreased activity of arginase and urease in the AM root. The catabolic activity of the urea cycle in the roots therefore depends on Arg translocation from the ERM. (15)N labeling of Arg in the ERM was very fast and analysis of its time course and isotopomer pattern allowed estimation of the translocation rate of Arg along the mycelium as 0.13 microg Arg mg(-1) fresh weight h(-1). The results highlight the synchronization of the spatially separated reactions involved in the anabolic and catabolic arms of the urea cycle. This synchronization is a prerequisite for Arg to be a key component in nitrogen translocation in the AM mycelium.

Arginine↗
PubMed1980

Changes in the regulatory form of Rhodospirillum rubrum nitrogenase as influenced by nutritional and environmental factors.

The photosynthetic bacterium Rhodospirillum rubrum regulates the activity of its nitrogenase (N2ase) by interconverting the enzyme into three distinct enzymatic species: N2ase A (a fully active form) and two regulatory forms, N2ase Ractive and N2ase Rinactive. N2ase R is distinguished from N2ase A in vitro by the requirement of its Fe protein for activation by a Mn2+-dependent activating factor. N2ase is converted from the A to the R form in response to certain environmental factors such as carbon starvation, depletion of intracellular adenosine triphosphate, or the addition of NH4+ (or glutamate) to a culture of N-starved cells. The rapid inhibition of R. rubrum N2ase in vivo by NH4+ was shown to result from the conversion of N2ase A to N2ase Rinactive. On depletion of NH4+ from the culture, whole-cell N2ase activity returned; however, the enzyme remained in the R form. Unlike the effect of NH4+, adding glutamate to cells containing N2ase A did not inhibit in vivo activity, but converted the enzyme to the R form (N2ase Ractive). Although glutamate-induced N2ase R formation was much slower than the NH4+-induced reaction, it occurred in the presence of rifampin, indicating that de novo protein synthesis was not involved. This suggested that N2ase R was formed by a modification of N2ase A. Although glutamine synthetase in involved in the conversion of N2ase A to R, the adenylylation state of glutamine synthetase appears not to be involved in regulating this nitrogenase reaction.

Carbon↗
PubMed2006

Changing chemical composition of precipitation in Wilmington, North Carolina, U.S.A.: implications for the Continental U.S.A.

The H+(aq) concentration in Wilmington, NC, precipitation has decreased by approximately 50% during the preceding two decades, similar to trends seen nationwide. The decrease in acidity is important because solution pH plays a key role in atmospheric reactions, and because the change is so large. This study presents the first long-range study of dissolved organic carbon (DOC) levels in precipitation which demonstrates that DOC concentrations have decreased by approximately half in Wilmington, NC, precipitation. The concentrations of H+(aq) and DOC are highly correlated primarily because small organic acids contribute to both DOC and H+(aq) in precipitation. Ammonium ion concentrations in precipitation have increased due to increased agricultural activities, and this also affects precipitation pH. The reduction of SO2 emissions in 1995 imposed by the Clean Air Act Amendment, better control of emissions of volatile organic compounds, and the increase in ammonia emissions all contribute to the decreasing H+(aq) in precipitation nationwide. These compositional changes in precipitation have many environmental implications, such as decreased acid deposition to lakes, changing speciation for trace metals in precipitation, increased ammonium deposition to coastal waters, and decreased DOC transport to the open ocean.

Acid Rain↗
PubMed2002

Molecular and enzymatic analysis of ammonium assimilation in woody plants.

Ammonium is assimilated into amino acids through the sequential action of glutamine synthetase (GS) and glutamate synthase (GOGAT) enzymes. This metabolic pathway is driven by energy, reducing power and requires the net supply of 2-oxoglutarate that can be provided by the reaction catalysed by isocitrate dehydrogenase (IDH). Most studies on the biochemistry and molecular biology of N-assimilating enzymes have been carried out on annual plant species and the available information on woody models is far more limited. This is in spite of their economic and ecological importance and the fact that nitrogen is a common limiting factor for tree growth. GS, GOGAT and IDH enzymes have been purified from several woody species and their kinetic and molecular properties determined. A number of cDNA clones have also been isolated and characterized. Although the enzymes are remarkably well conserved along the evolutionary scale, major differences have been found in their compartmentation within the cell between angiosperms and conifers, suggesting possible adaptations to specific functional roles. The analysis of the gene expression patterns in a variety of biological situations such as changes in N nutrition, development, biotic or abiotic stresses and senescence, suggest that cytosolic GS plays a central and pivotal role in ammonium assimilation and metabolism in woody plants. The modification of N assimilation efficiency has been recently approached in trees by overexpression of a cytosolic pine GS in poplar. The results obtained, suggest that an increase in cytosolic GS might lead to a global effect on the synthesis of nitrogenous compounds in the leaves, with enhanced vegetative growth of transgenic trees. All these data suggest that manipulation of cytosolic GS may have consequences for plant growth and biomass production.

Amino Acid Oxidoreductases↗
PubMed1979

[Metabolism of ammonium compounds by Azotobacter chroococcum (author's transl)].

A study on the metabolism of ammonium sulphate, amino acids, peptides, and nutrient broth by Azotobacter chroococcum is presented in this paper. Some of the amino acids studied lowered the pH of the medium while others alkalinized it. After prolonged incubation desamination could be observed. Peptides were hydrolyzed in some cases, although glycyl-glycyl-glycin was not degraded. A certain amount of growth could be observed with peptone as a sole source of carbon. Both nitrogen fixation and growth were stimulated by nutrient broth, but the medium was alkalinized when a higher concentration of nutrient broth was used, due to the production of ammonia.

Amines↗
PubMed2003

Powdered activated carbon added biological treatment of pre-treated landfill leachate in a fed-batch reactor.

Biological treatment of landfill leachate usually results in low treatment efficiencies because of high chemical oxygen demand (COD), high ammonium-N content and also presence of toxic compounds such as heavy metals. A landfill leachate with high COD content was pre-treated by coagulation-flocculation followed by air stripping of ammonia at pH = 12. Pre-treated leachate was biologically treated in an aeration tank operated in fed-batch mode with and without addition of powdered activated carbon (PAC). PAC at 2 g l-1 improved COD and ammonium-N removals resulting in nearly 86% COD and 26% NH4-N removal.

Bacteria, Aerobic↗
PubMed1984

Covalent modification of bacterial glutamine synthetase: physiological significance.

Stadtman, Holzer and their colleagues (reviewed in Stadtman and Ginsburg 1974) demonstrated that the enzyme glutamine synthetase (GS) [(L-glutamate: ammonia ligase (ADP-forming), EC 6.3.1.2] is covalently modified by adenylylation in a variety of bacterial genera and that the modification is reversible. These studies further indicated that adenylylated GS is the less active form in vitro. To assess the physiological significance of adenylylation of GS we have determined the growth defects of mutant strains (glnE) of S. typhimurium that are unable to modify GS and we have determined the basis for these growth defects. The glnE strains, which lack GS adenylyl transferase activity (ATP: [L-glutamate: ammonia ligase (ADP-forming)] adenylyltransferase, EC 2.7.7.42), show a large growth defect specifically upon shift from a nitrogen-limited growth medium to medium containing excess ammonium (NH4+). The growth defect appears to be due to very high catalytic activity of GS after shift, which lowers the intracellular glutamate pool to approximately 10% that under preshift conditions. Consistent with this view, recovery of a rapid growth rate on NH4+ is accompanied by an increase in the glutamate pool. The glnE strains have normal ATP pools after shift. They synthesize very large amounts of glutamine and excrete glutamine into the medium, but excess glutamine does not seem to inhibit growth. We hypothesize that a major function for adenylylation of bacterial GS is to protect the cellular glutamate pool upon shift to NH4+ -excess conditions and thereby to allow rapid growth.

Bacterial Proteins↗
PubMed1984

Some properties of a Klebsiella pneumoniae ammonium transport negative mutant (Amt-).

The main property of an Amt- (ammonium transport negative) mutant of Klebsiella pneumoniae is its inability to accumulate NH4+ intracellularly. When growing on nitrogen sources other than NH4+, the mutant constantly looses NH3 by diffusion. This loss results in poor growth. The NH3 excretion suggests the existence of a futile cycle (NH3 loss/NH4+ reabsorption) in the wild type and possibly other bacterial strains, which do not constantly excrete NH3.

Ammonia↗
PubMed1976

Photoproduction of ammonium ion from N2 in Rhodospirillum rubrum.

NH+4 excretion was undetectable in N2-fixing cultures of Rhodospirillum rubrum (S-1) and nitrogenase activity in these cultures was repressed by the addition of 10 mM NH+4 to the medium. The glutamate analog, L-methionine-DL-sulfoximine (MSX), derepressed N2 fixation even in the presence of 10 mM extracellular NH+4. When 10 mg MSX/ml was added to cultures just prior to nitrogenase induction they developed nitrogenase activity (20% of the control activities) and excreted most of their fixed N2 as NH+4. Nitrogenase activities and NH+4 production from fixed N2 were increased considerably when a combined nitrogen source, NH+4 (greater than 40 mumoles NH+4/mg cell protein in 6 days) or L-glutamate (greater than 60 mumoles NH+4/ mg cell protein in 6 days) was added to the cultures together with MSX. Biochemical analysis revealed that R. rubrum produced glutamine synthetase and glutamate synthase (NADP-dependent) but no detectable NADP-dependent glutamate dehydrogenase. The specific activity of glutamine synthetase was observed to be maximal when nitrogenase activity was also maximal. Nitrogenase and glutamine synthetase activities were repressed by NH+4 as well as by glutamate. The results demonstrate that utilization of solar energy to photoproduce large quantities of NH+4 from N2 is possible with photosynthetic bacteria by interfering with their regulatory control of N2 fixation.

Glutamate Dehydrogenase↗
PubMed2006

Glutamate is involved in acid stress response in Bradyrhizobium sp. SEMIA 6144 (Arachis hypogaea L.) microsymbiont.

In the present study, the effect of acid stress on ammonium assimilation in Bradyrhizobium sp. SEMIA 6144 (Arachis hypogaea L.) microsymbiont was analyzed. The bacterial growth rate was decreased by 50%, and a significant increase in intracellular glutamate concentration was detected when the strain grew at acid pH (5.5). Assays of the enzymes involved in glutamate synthesis showed increased activities of glutamine synthetase (GS) and glutamate synthase (NADPH-GOGAT) under acid stress condition. This would support the contention that the GS/NADPH-GOGAT pathway contributes to the increase of glutamate synthesis as a compatible solute in response to acid stress.

Acids↗
PubMed1984

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.

Enzyme Activation↗
PubMed1996

Participation of NH4+ in total ammonia absorption across the rumen epithelium of sheep (Ovis aries).

1. Participation of NH4+ in total ammonia transport across sheep rumen wall was studied in vitro. 2. In Ussing-type chambers addition of NH4+ or K+ to the incubation solution on the mucosal side of the epithelium evoked positive short-circuit currents (ISC). 3. The K+ induced ISC but not the NH4+ induced ISC could be blocked by Ba2+ whereas both, K+ or NH4+ induced ISC were blocked by quinidine. 4. Transepithelial fluxes of ammonia were significantly reduced when quinidine was present in the incubation solution. 5. When the transepithelial potential difference was clamped to -25 mV (polarity on the serosal side) ammonia fluxes from the mucosal to the serosal side were significantly larger than fluxes of ammonia measured as a potential difference of +25 mV. 6. It is suggested that NH4+ takes part in ammonia transport across the rumen epithelium, most probably by using a K(+)-transport system.

Ammonia↗