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PubMed1993

Glutamine Involvement in Nitrogen Control of Gibberellic Acid Production in Gibberella fujikuroi.

When the fungus Gibberella fujikuroi ATCC 12616 was grown in fermentor cultures, both intracellular kaurene biosynthetic activities and extracellular GA(3) accumulation reached high levels when exogenous nitrogen was depleted in the culture. Similar patterns were exhibited by several nonrelated enzymatic activities, such as formamidase and urease, suggesting that all are subject to nitrogen regulation. The behavior of the enzymes involved in nitrogen assimilation (glutamine synthetase, glutamate dehydrogenase, and glutamate synthase) during fungal growth in different nitrogen sources suggests that glutamine is the final product of nitrogen assimilation in G. fujikuroi. When ammonium or glutamine was added to hormone-producing cultures, extracellular GA(3) did not accumulate. However, when the conversion of ammonium into glutamine was inhibited by L-methionine-DL-sulfoximine, only glutamine maintained this effect. These results suggest that glutamine may well be the metabolite effector in nitrogen repression of GA(3) synthesis, as well as in other nonrelated enzymatic activities in G. fujikuroi.

Journal Article↗

PubMed2006

Feedback-resistant mutations in Bacillus subtilis glutamine synthetase are clustered in the active site.

The feedback-inhibited form of Bacillus subtilis glutamine synthetase regulates the activity of the TnrA transcription factor through a protein-protein interaction that prevents TnrA from binding to DNA. Five mutants containing feedback-resistant glutamine synthetases (E65G, S66P, M68I, H195Y, and P318S) were isolated by screening for colonies capable of cross-feeding Gln(-) cells. In vitro enzymatic assays revealed that the mutant enzymes had increased resistance to inhibition by glutamine, AMP, and methionine sulfoximine. The mutant proteins had a variety of enzymatic alterations that included changes in the levels of enzymatic activity and in substrate K(m) values. Constitutive expression of TnrA- and GlnR-regulated genes was seen in all five mutants. In gel mobility shift assays, the E65G and S66P enzymes were unable to inhibit TnrA DNA binding, while the other three mutant proteins (M68I, H195Y, and P318S) showed partial inhibition of TnrA DNA binding. A homology model of B. subtilis glutamine synthetase revealed that the five mutated amino acid residues are located in the enzyme active site. These observations are consistent with the hypothesis that glutamine and AMP bind at the active site to bring about feedback inhibition of glutamine synthetase.

Bacillus subtilis↗

PubMed1973

Comparative biochemical and immunological studies of bacterial glutamine synthetases.

Antisera prepared against adenylylated and unadenylylated Escherichia coli glutamine synthetase cross-reacted with the glutamine synthetases from a number of gram-negative bacteria and one gram-variable species as demonstrated by immunodiffusion and inhibition of enzyme activity. In contrast, the antisera did not cross-react with the glutamine synthetases from gram-positive bacteria (with one exception) nor with the synthetases of higher organisms. Modification of the various glutamine synthetases by covalent attachment of adenosine 5'-monophosphate (or other nucleotides) was tested for by determining whether or not snake venom phosphodiesterase altered catalytic activity in a manner similar to its effect on adenylylated E. coli glutamine synthetase. Only the activity of the glutamine synthetases from gram-negative bacteria grown with specific levels of nitrogen sources could be altered by snake venom phosphodiesterase. In addition, a relative order of antigenic homology between cross-reacting enzymes was suggested based on the patterns of spur formation in the immunodiffusion assay.

Adenine Nucleotides↗

PubMed1977

Autogenous regulation of the synthesis of glutamine synthetase in Klebsiella aerogenes.

We isolated an F' episome of Escherichia coli carrying the glnA+ gene from K. aerogenes and an F' episome of E. coli carrying the glnA4 allele from K. aerogenes responsible for the constitutive synthesis of glutamine synthetase. Complementation tests with these episomes showed that the glnA4 mutation (leading to the constitutive synthesis of active glutamine synthetase) was in the gene identified by mutations glnA20, glnA51, and glnA5 as the structural gene for glutamine synthetase. By using these merodiploid strains we were able to show that the glnA51 mutation lead to the synthesis of a glutamine synthetase that lacked enzymatic activity but fully retained its regulatory properties. Finally, we discuss a model that explains the several phenotypes associated with mutations such as glnA4 located within the structural gene for glutamine synthetase leading to constitutive synthesis of active glutamine synthetase.

Alleles↗

PubMed1981

Glutamine synthetase of pseudomonads: some biochemical and physicochemical properties.

The glutamine synthetases from several Pseudomonas species were purified to homogeneity, and their properties were compared with those reported for the enzymes from Escherichia coli and other gram-negative bacteria. The glutamine synthetase from Pseudomonas fluorescens was unique because it was nearly precipitated quantitatively as a homogeneous protein during dialysis of partially purified preparations against buffer containing 10 mM imidazole (pH 7.0) and 10 mM MnCl2. The glutamine synthetases from Pseudomonas putida and Pseudomonas aeruginosa were purified by affinity chromatography on Affi-blue gel. Dodecamerous forms of the E. coli and P. fluorescens glutamine synthetases had identical mobilities during polyacrylamide gel electrophoresis. Their dissociated subunits, however, migrated differently and were readily separated by electrophoresis on polyacrylamide gels containing 0.1% sodium dodecyl sulfate. This difference in subunit mobilities is not related to the state of adenylylation. Regulation of the Pseudomonas glutamine synthetase activity is mediated by an adenylylation-deadenylylation cyclic cascade system. A sensitive procedure was developed for measuring the average number of adenylylated subunits per enzyme molecule for the glutamine synthetase from P. fluorescens. This method takes advantage of the large differences in transferase activity of the adenylylated and unadenylylated subunits at pH 6.0 and of the fact that the activities of both kinds of subunits are the same at pH 8.45.

Adenosine Monophosphate↗

PubMed1983

Role of glutamine synthetase in the uptake and metabolism of methylammonium by Azotobacter vinelandii.

Methylammonium is a substrate for the ammonium transport system of Azotobacter vinelandii. During cellular uptake methylammonium is rapidly converted to a less polar metabolite (E. M. Barnes, Jr., and P. Zimniak, J. Bacteriol. 146:512-516, 1981). This metabolite has been isolated from A. vinelandii and identified as gamma-glutamylmethylamide by mass spectroscopy, 1H nuclear magnetic resonance spectroscopy, and cochromatography with the authentic compound. Escherichia coli also accumulated gamma-glutamylmethylamide during methylammonium uptake. The biosynthesis of gamma-glutamylmethylamide in vitro required methylammonium, ATP, L-glutamate, and a soluble cell extract from A. vinelandii. The enzyme responsible for gamma-glutamylmethylamide synthesis was glutamine synthetase. In a crude extract, L-methionine-DL-sulfoximine was equipotent in inhibiting the activities for gamma-glutamyltransferase and for the synthesis of glutamine and gamma-glutamylmethylamide. Likewise, an antiserum against the glutamine synthetase of E. coli precipitated the transferase and both synthetic activities at similar titers. During repression by growth of cells on ammonium medium, the synthesis of glutamine and gamma-glutamylmethylamide in vitro was also inhibited coordinately. A partially purified preparation of glutamine synthetase from A. vinelandii utilized methylammonium as substrate (Km = 78 mM, Vmax = 0.30 mumol/min per mg), although less efficiently than ammonium (Km = 0.089 mM, Vmax = 1.1 mumol/min per mg). The kinetic properties of glutamine synthetase with methylammonium as substrate as well as the insensitivity of this activity to inhibition by T1+ were strikingly different from methylammonium translocation. Thus, methylammonium (ammonium) translocation and intracellular trapping as glutamylamides are experimentally distinguishable processes.

Azotobacter↗

PubMed1984

Expression of the Bacillus subtilis glutamine synthetase gene in Escherichia coli.

The structural gene for glutamine synthetase (glnA) in Bacillus subtilis ( glnAB ) cloned in the lambda vector phage Charon 4A was used to transduce a lysogenic glutamine auxotrophic Escherichia coli strain to prototrophy. The defective E. coli gene ( glnAE ) was still present in the transductant since it could be transduced. In addition, curing of the prototroph resulted in the restoration of glutamine auxotrophy. Proteins in crude extracts of the transductant were examined by a "Western blotting" procedure for the presence of B. subtilis or E. coli glutamine synthetase antigen; only the former was detected. Growth of the strain in media without glutamine was not curtailed even when the bacteriophage lambda pL and pRM promoters were hyperrepressed . The specific activities and patterns of derepression of glutamine synthetase in the transductant were similar to those of B. subtilis, with no evidence for adenylylation. The information necessary for regulation of glnAB must be closely linked to the gene and appears to function in E. coli.

Bacillus subtilis↗

PubMed1985

Molecular and regulatory properties of glutamine synthetase from the phototrophic bacterium Rhodopseudomonas capsulata E1F1.

The glutamine synthetase of the phototrophic bacterium Rhodopseudomonas capsulata E1F1 was purified to homogeneity by a procedure which used a single affinity chromatography step. Like enzymes from other photosynthetic procaryotes, native glutamine synthetase from R. capsulata E1F1 was found to be a dodecameric protein of approximately 660 kilodaltons with identical subunits of about 55 kilodaltons each. The Stokes radius and S20,w of the native enzyme were 8.35 nm and 19.20, respectively. The enzyme exhibited different aggregation states with detectable oligomers of 1, 2, 3, 4, 6, 8, 10, and 12 subunits. Disaggregation of the glutamine synthetase occurred after the native protein was subjected to electrophoresis in polyacrylamide gels, as well as occurring spontaneously at low ionic strength. Glutamine synthetase from R. capsulata E1F1 was regulated by an adenylylation-deadenylylation mechanism, and the adenylylation state of the protein depended on the nitrogen source, growth phase, and light intensity. Ammonia repressed glutamine synthetase, whereas glycine, serine, alanine, valine, and aspartate were noncompetitive inhibitors of the glutamine synthetase biosynthetic activity.

Adenine Nucleotides↗

PubMed1990

Molecular analysis of the Azotobacter vinelandii glnA gene encoding glutamine synthetase.

The gene encoding glutamine synthetase (GS), glnA, was cloned from Azotobacter vinelandii on a 6-kb EcoRI fragment that also carries the ntrBC genes. The DNA sequence of 1,952 bp including the GS-coding region was determined. An open reading frame of 467 amino acids indicated a gene product of Mr 51,747. Transcription of glnA occurred from a C residue located 32 bases upstream of an ATG considered to be the initiator codon because (i) it had a nearby potential ribosome-binding site and (ii) an open reading frame translated from this site indicated good N-terminal homology to 10 other procaryotic GSs. Sequences similar to the consensus RNA polymerase recognition sites at -10 and -35 were present at the appropriate distance upstream of the transcription initiation site. As expected from earlier genetic studies indicating that expression of A. vinelandii glnA did not depend on the rpoN (ntrA; sigma 54) gene product, no sigma 54 recognition sequences were present, nor was there significant regulation of glnA expression by fixed nitrogen. Repeated attempts to construct glutamine auxotrophs by recombination of glnA insertion mutations were unsuccessful, Although the mutated DNA could be found by hybridization experiments in drug-resistant A. vinelandii transformants, the wild-type glnA region was always present. These results suggest that glnA mutations are lethal in A. vinelandii. In [14C]glutamine uptake experiments, very little glutamine was incorporated into cells, suggesting that glutamine auxotrophs are nonviable because they cannot be supplied with sufficient glutamine to support growth.

Amino Acid Sequence↗

PubMed1994

The femC locus of Staphylococcus aureus required for methicillin resistance includes the glutamine synthetase operon.

Tn551 insertional inactivation of femC is known to reduce methicillin resistance levels in methicillin-resistant and -susceptible Staphylococcus aureus. By use of cotransductional crosses, femC was mapped close to thrB on the SmaI-A fragment of the S. aureus NCTC 8325 chromosome. The Tn551 insertion femC::omega 2005 was found to interrupt an open reading frame coding for a putative protein of 121 amino acids which is highly similar to the glutamine synthetase repressors (GlnR) of Bacillus spp. Downstream of femC, an open reading frame highly similar to Bacillus sp. glutamine synthetases (GlnA) was found. Northern (RNA) blots probed with putative glnR or glnA fragments revealed that 1.7- and 1.9-kb transcripts characteristic of wild-type cells were replaced by less abundant 7.0- and 7.2-kb transcripts in the femC::omega 2005 mutant. Total glutamine synthetase activity was also decreased in the mutant strain; the addition of glutamine to defined media restored the wild-type methicillin resistance phenotype of the femC mutant. This result suggests that the omega 2005 insertion in glnR has a polar effect on glnA and that glnR and glnA are transcribed together as an operon. These results suggest that the loss of wild-type levels of glutamine synthetase and the consequent decrease in glutamine availability cause a decreased level of methicillin resistance.

Amino Acid Sequence↗

PubMed1985

Influence of nitrogen source and growth status on glutamine synthetase and glutamate synthase activity in Mycobacterium avium.

An investigation was made of the activity of glutamine synthetase and glutamate synthase from batch-cultured cells of Mycobacterium avium. The bacteria were grown in medium with ammonium chloride concentrations of 0, 0.1, 0.25, 1, 5, or 25 mumol/mL or with glutamine at 0.1 or 1 mumol/mL. The specific activity of the two enzymes was determined at 0, 22, 45, and 70 h of incubation. Regardless of the ammonia concentration in the medium, glutamate synthase specific activity was two to five times higher in extracts from elongating cells, incubated 22 h, than in those from shortened cells, incubated 45 or 70 h. In contrast, there was no apparent difference in glutamine synthetase specific activity with regard to culture age; however, glutamine synthetase specific activity varied inversely with the concentration of ammonium chloride in the medium. Cells grown in glutamine had high activity of glutamine synthetase.

Ammonium Chloride↗

PubMed2004

Glutamine kinetics and protein turnover in end-stage renal disease.

Alanine and glutamine constitute the two most important nitrogen carriers released from the muscle. We studied the intracellular amino acid transport kinetics and protein turnover in nine end-stage renal disease (ESRD) patients and eight controls by use of stable isotopes of phenylalanine, alanine, and glutamine. The amino acid transport kinetics and protein turnover were calculated with a three-pool model from the amino acid concentrations and enrichment in the artery, vein, and muscle compartments. Muscle protein breakdown was more than synthesis (nmol.min(-1).100 ml leg(-1)) during hemodialysis (HD) (169.8 +/- 20.0 vs. 125.9 +/- 21.8, P < 0.05) and in controls (126.9 +/- 6.9 vs. 98.4 +/- 7.5, P < 0.05), but synthesis and catabolism were comparable pre-HD (100.7 +/- 15.7 vs. 103.4 +/- 14.8). Whole body protein catabolism decreased by 15% during HD. The intracellular appearance of alanine (399.0 +/- 47.1 vs. 243.0 +/- 34.689) and glutamine (369.7 +/- 40.6 vs. 235.6 +/- 27.5) from muscle protein breakdown increased during dialysis (nmol.min(-1).100 ml leg(-1), P < 0.01). However, the de novo synthesis of alanine (3,468.9 +/- 572.2 vs. 3,140.5 +/- 467.7) and glutamine (1,751.4 +/- 82.6 vs. 1,782.2 +/- 86.4) did not change significantly intradialysis (nmol.min(-1).100 ml leg(-1)). Branched-chain amino acid catabolism (191.8 +/- 63.4 vs. -59.1 +/- 42.9) and nonprotein glutamate disposal (347.0 +/- 46.3 vs. 222.3 +/- 43.6) increased intradialysis compared with pre-HD (nmol.min(-1).100 ml leg(-1), P < 0.01). The mRNA levels of glutamine synthase (1.45 +/- 0.14 vs. 0.33 +/- 0.08, P < 0.001) and branched-chain keto acid dehydrogenase-E2 (3.86 +/- 0.48 vs. 2.14 +/- 0.27, P < 0.05) in the muscle increased during HD. Thus intracellular concentrations of alanine and glutamine are maintained during HD by augmented release of the amino acids from muscle protein catabolism. Although muscle protein breakdown increased intradialysis, the whole body protein catabolism decreased, suggesting central utilization of amino acids released from skeletal muscle.

Adult↗

PubMed1990

Effect of diabetes on glutamine synthetase expression in rat skeletal muscles.

The regulation of glutamine synthetase expression in muscles from normal and diabetic (streptozotocin-treated) rats was studied. Muscle and body weights were markedly reduced in diabetic animals. Glutamine synthetase activity was significantly (2-fold) elevated 7 days after induction of diabetes. Increased enzyme activity persisted for at least 14 days after induction of diabetes, and it was apparent in both slow (soleus) and fast (plantaris) muscles. The diabetes-induced increase in enzyme activity was reflected in an increased steady-state level of glutamine synthetase mRNA. The increases in glutamine synthetase activity and mRNA level in muscle from diabetic rats were reversed by insulin administration. Increased expression of glutamine synthetase may be important for accelerated glutamine production by muscle from diabetic rats.

Adrenalectomy↗

PubMedDate not supplied

The effect of preventive use of alanyl-glutamine on diaphragm muscle function in cecal ligation and puncture-induced sepsis model.

BACKGROUND: Low muscle glutamine levels during sepsis are associated with reduced protein synthesis and elevated protein breakdown, in particular myofibrillar protein breakdown. Thus, in a cecal ligation and puncture (CLP)-induced sepsis model in the rat, we hypothesized that glutamine pretreatment would protect the diaphragm muscle function. METHODS: Eighty-four male Wistar rats weighing between 180 g and 200 g received standard amino acid solution 1.2 g kg(-1) per day intraperitoneally (IP) or standard amino acid solution 1.2 g kg(-1) per day plus alanyl-glutamine (GLN) 0.25 g kg(-1) per day (IP) during the first 6 days of the experiment. On the seventh day, CLP or sham procedures were applied. The sham and CLP groups were equally divided into 3 subgroups according to the termination of the experiment, which took place at either the 24th hour, 48th hour, or 72nd hour. After the compound muscle action potentials (CMAP) were recorded from the diaphragms of the rats at these selected times, they were decapitated under ketamine/xylazine anesthesia, and diaphragms were harvested for biochemical and histopathological examination. RESULTS: The mean area and amplitude of CMAP were significantly larger in sham+GLN groups when compared with CLP and CLP+GLN groups at all times (p < .05). Diaphragm Ca+2 -ATPase levels were found to be significantly decreased in CLP group at all times compared to sham groups (p < .05). Diaphragm reduced glutathione levels were significantly higher in sham+GLN groups when compared with CLP and CLP+GLN groups at all times (p < .05). In histopathologic assessment, moderate neutrophil infiltration, which was observed in CLP48, was significantly reduced with alanyl-glutamine supplementation in CLP+GLN48 group (p < .05). CONCLUSIONS: This study showed that glutamine pretreatment did not improve diaphragm muscle function, but prevented the biochemical and histopathological changes in diaphragmatic muscle in CLP-induced sepsis. However, further studies are needed to clarify whether a higher dose of glutamine supplementation might protect the diaphragmatic muscle functions.

Action Potentials↗

PubMedDate not supplied

Cerebrospinal and plasma amino acid concentrations after administration of i.v. glycyl-glutamine and glycyl-tyrosine containing amino acid solutions in humans.

BACKGROUND: Glycyl-glutamine and glycyl-tyrosine may supply adequate glutamine and tyrosine in amino acid solutions for parenteral nutrition. However, plasma peptides may be transported into the cerebrospinal fluid, exerting effects on the neuronal tissue. Cerebrospinal fluid (CSF) and plasma amino acid concentrations after administration of a glycyl-glutamine/glycyltyrosine supplemented amino acid solution were therefore evaluated in a randomized controlled comparison with a conventional amino acid infusion. METHODS: Dipeptide/amino acid solutions (0.60 mL/h/kg; 82.2 mg total dipeptides/amino acids/h/kg) or conventional amino acid solutions (0.73 mL/h/kg; 83.2 mg total amino acids/h/kg) were infused in 15 patients per group scheduled to undergo spinal anesthesia for urologic surgery over a 12-hour period preoperatively. Plasma amino acids were measured before the infusion was started. CSF and venous concentrations were analyzed simultaneously before the infusion was stopped. CSF samples were drawn through the spinal needle for anesthesia. RESULTS: The dipeptide-containing solution did not increase either dipeptide to detectable levels in the CSF (detection limit < 5.0 nmol/mL). Venous glycyl-glutamine increased from below detection limits up to 308 +/- 111 nmol/mL (p < .05), whereas glycyl-tyrosine could not be found. In the dipeptide group, venous glutamine and tyrosine were higher (p < .05) but only tyrosine appeared in small amounts (p < .05) in the cerebrospinal fluid. CONCLUSIONS: This study provides no evidence to support a CSF entry of IV glycyl-tyrosine and glycyl-glutamine under conditions of a normal blood-brain barrier in the adult (detection limit 5 nmol/mL). The data suggest that amino acid solutions containing these dipeptides may be used in parenteral solutions for nutrition support.

Aged↗

PubMed1987

Heterogeneous distribution of glutamine synthetase during rat liver development.

Two days before birth, immunohistochemical detection of glutamine synthetase already reveals a heterogeneous distribution pattern related to the vascular architecture of the liver. Only a small number of hepatocytes in the vicinity of the efferent venules show relatively high staining intensity. Before that age, only megakaryocytes show intense staining, while liver parenchyma is only faintly stained. The developmental profile of glutamine synthetase activity shows two periods of increasing enzyme activity: one in the perinatal period and one in the second and third postnatal week. Both periods are correlated with high levels of circulating corticosteroid hormones. Although the relative number of intensely stained hepatocytes increases during the first rise in enzyme activity, the second rise is correlated with a decreasing number of glutamine synthetase-positive hepatocytes which, however, show a considerable increase in staining intensity. Carbamoylphosphate synthetase shows a homogeneous distribution pattern in the perinatal period. Conditions that lead during development to a relatively high level of glutamine synthetase expression in the pericentral compartment apparently originate before the appearance of conditions that lead to a relatively high level of carbamoylphosphate synthetase gene expression in the periportal compartment. Our results indicate that downstream localization of glutamine synthetase in liver acinus is essential from the perinatal period onwards, whereas reciprocal distribution of glutamine synthetase and carbamoylphosphate synthetase gene expression (that is found in adult rat liver) is not.

Animals↗

PubMed2005

Induction and targeting of the glutamine transporter SN1 to the basolateral membranes of cortical kidney tubule cells during chronic metabolic acidosis suggest a role in pH regulation.

During chronic metabolic acidosis (CMA), the plasma levels of glutamine are increased and so is glutamine metabolism in the kidney tubule cells. Degradation of glutamine results in the formation of ammonium (NH(4)(+)) and bicarbonate (HCO(3)(-)) ions, which are excreted in the pre-urine and transported to the peritubular blood, respectively. This process contributes to counteract acidosis and to restore normal pH, but the molecular mechanism, the localization of the proteins involved and the regulation of glutamine transport into the renal tubular cells, remains unknown. SN1, a Na(+)- and H(+)-dependent glutamine transporter has previously been identified molecularly, and its mRNA has been detected in tubule cells in the medulla of the kidney. Now shown is the selective targeting of the protein to the basolateral membranes of the renal tubule cells of the S3 segment throughout development of the normal rat kidney. During CMA, SN1 expression increases five- to six-fold and appears also in cortical tubule cells in parallel with the increased expression and activity of phosphate-activated glutaminase, a mitochondrial enzyme involved in ammoniagenesis. However, SN1 remains sorted to the basolateral membranes. The unique ability of SN1 to change transport direction according to physiologic changes in transmembrane gradients of [glutamine] and pH and its sorting to the basolateral membranes and the presence of a putative pH responsive element in the 3' untranslated region (UTR) of the gene (supported here by the demonstration in CMA kidney of a protein that binds SN1 mRNA) are conducive to the function of this transporter in pH regulation.

Acidosis↗

PubMed1999

[Glutamine as a key ingredient in protein metabolism].

Glutamine has a number of unique properties which suggest that this amino acid plays an important role in health and disease. Glutamine is considered a conditionally essential amino acid, because during periods of severe metabolic stress the body's requirements of glutamine may exceed the individual's ability to produce sufficient amounts of the amino acid. Studies with glutamine-enriched nutrition show beneficial effects on nitrogen balance, muscle protein metabolism, gastrointestinal mucosa, and immune status. In certain patient categories addition of glutamine reduces the number of infectious complications, improves long-term survival, and shortens hospital stay, e.g. bone marrow transplantation patients, neonates with severely subnormal weight, patients with multiple organ failure, multi-trauma patients. More studies are needed to document the dose-response and to identify the patients that are likely to benefit from glutamine supplementation.

Amino Acids, Essential↗