Glutamine. Medical search

A non-essential amino acid present abundantly throughout the body and is involved in many metabolic processes. It is synthesized from GLUTAMIC ACID and AMMONIA. It is the principal carrier of NITROGEN in the body and is an important energy source for many cells.

An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC 6.3.1.2.

A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.

An amino acid that inhibits phosphate-activated glutaminase and interferes with glutamine metabolism. It is an antineoplastic antibiotic produced by an unidentified species of Streptomyces from Peruvian soil. (From Merck Index, 11th ed)

Derivatives of GLUTAMIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the 2-aminopentanedioic acid structure.

A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.

An enzyme that catalyzes the formation of 2 molecules of glutamate from glutamine plus alpha-ketoglutarate in the presence of NADPH. EC 1.4.1.13.

Stable nitrogen atoms that have the same atomic number as the element nitrogen, but differ in atomic weight. N-15 is a stable nitrogen isotope.

A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)

An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.

An enzyme, involved in the early steps of purine nucleotide biosynthesis, that catalyzes the formation of 5-phosphoribosylamine from glutamine and phosphoribosylpyrophosphate. EC 2.4.2.14.

A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.

Enzymes that catalyze the transfer of nitrogenous groups, primarily amino groups, from a donor, generally an amino acid, to an acceptor, usually a 2-oxoacid. EC 2.6.

One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.

The rate dynamics in chemical or physical systems.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

An enzyme that catalyzes the synthesis of fructose-6-phosphate plus GLUTAMINE from GLUTAMATE plus glucosamine-6-phosphate.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

A subclass of enzymes of the transferase class that catalyze the transfer of an amino group from a donor (generally an amino acid) to an acceptor (generally a 2-keto acid). Most of these enzymes are pyridoxyl phosphate proteins. (Dorland, 28th ed) EC 2.6.1.

A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)

Amino acid transporter systems capable of transporting neutral amino acids (AMINO ACIDS, NEUTRAL).

Derivatives of ammonium compounds, NH4+ Y-, in which all four of the hydrogens bonded to nitrogen have been replaced with hydrocarbyl groups. These are distinguished from IMINES which are RN=CR2.

A transfer RNA which is specific for carrying glutamine to sites on the ribosomes in preparation for protein synthesis.

A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.

A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.

Antibiotic substance produced by various Streptomyces species. It is an inhibitor of enzymatic activities that involve glutamine and is used as an antineoplastic and immunosuppressive agent.

A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.

An enzyme that catalyzes the formation of anthranilate (o-aminobenzoate) and pyruvic acid from chorismate and glutamine. Anthranilate is the biosynthetic precursor of tryptophan and numerous secondary metabolites, including inducible plant defense compounds. EC 4.1.3.27.

Elevated level of AMMONIA in the blood. It is a sign of defective CATABOLISM of AMINO ACIDS or ammonia to UREA.

A ubiquitous sodium-dependent neutral amino acid transporter. The preferred substrates for this transporter system include ALANINE; SERINE; and CYSTEINE.

A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.

An acidifying agent that has expectorant and diuretic effects. Also used in etching and batteries and as a flux in electroplating.

An amino acid produced in the urea cycle by the splitting off of urea from arginine.

An essential amino acid that is physiologically active in the L-form.

An essential branched-chain amino acid important for hemoglobin formation.

Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.

The delivery of nutrients for assimilation and utilization by a patient whose sole source of nutrients is via solutions administered intravenously, subcutaneously, or by some other non-alimentary route. The basic components of TPN solutions are protein hydrolysates or free amino acid mixtures, monosaccharides, and electrolytes. Components are selected for their ability to reverse catabolism, promote anabolism, and build structural proteins.

Nutritional support given via the alimentary canal or any route connected to the gastrointestinal system (i.e., the enteral route). This includes oral feeding, sip feeding, and tube feeding using nasogastric, gastrostomy, and jejunostomy tubes.

Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).

Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.

An enzyme that catalyzes the first step of histidine catabolism, forming UROCANIC ACID and AMMONIA from HISTIDINE. Deficiency of this enzyme is associated with elevated levels of serum histidine and is called histidinemia (AMINO ACID METABOLISM, INBORN ERRORS).

An amino acid formed in vivo by the degradation of dihydrouracil and carnosine. Since neuronal uptake and neuronal receptor sensitivity to beta-alanine have been demonstrated, the compound may be a false transmitter replacing GAMMA-AMINOBUTYRIC ACID. A rare genetic disorder, hyper-beta-alaninemia, has been reported.

A sodium-dependent neutral amino acid transporter that accounts for most of the sodium-dependent neutral amino acid uptake by mammalian cells. The preferred substrates for this transporter system include ALANINE; SERINE; and GLUTAMINE.

Transglutaminases catalyze cross-linking of proteins at a GLUTAMINE in one chain with LYSINE in another chain. They include keratinocyte transglutaminase (TGM1 or TGK), tissue transglutaminase (TGM2 or TGC), plasma transglutaminase involved with coagulation (FACTOR XIII and FACTOR XIIIa), hair follicle transglutaminase, and prostate transglutaminase. Although structures differ, they share an active site (YGQCW) and strict CALCIUM dependence.

Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.

The administering of nutrients for assimilation and utilization by a patient who cannot maintain adequate nutrition by enteral feeding alone. Nutrients are administered by a route other than the alimentary canal (e.g., intravenously, subcutaneously).

A compound that inhibits aminobutyrate aminotransferase activity in vivo, thereby raising the level of gamma-aminobutyric acid in tissues.

A family of signal transducing adaptor proteins that control the METABOLISM of NITROGEN. They are primarily found in prokaryotes.

An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and glutamine. This enzyme is important in the de novo biosynthesis of pyrimidines. EC 6.3.5.5.

Role of glutamine in human carbohydrate metabolism in kidney and other tissues. (1/3706)

Glutamine is the most abundant amino acid in the human body and is involved in more metabolic processes than any other amino acid. Until recently, the understanding of many aspects of glutamine metabolism was based on animal and in vitro data. However, recent studies using isotopic and balance techniques have greatly advanced the understanding of glutamine metabolism in humans and its role in glucose metabolism in the kidney and other tissues. There is now evidence that in postabsorptive humans, glutamine is an important glucose precursor and makes a significant contribution to the addition of new carbon to the glucose carbon pool. The importance of alanine for gluconeogenesis, viewed in terms of the addition of new carbons, is less than previously assumed. It appears that glutamine is predominantly a renal gluconeogenic substrate, whereas alanine gluconeogenesis is essentially confined to the liver. As shown recently, renal gluconeogenesis contributes 20 to 25% to whole-body glucose production. Moreover, glutamine has been shown not only to stimulate net muscle glycogen storage but also to stimulate gluconeogenesis in normal humans. Finally, in humans with type II diabetes, conversion of glutamine to glucose is increased (more so than that of alanine). The available evidence on the hormonal regulation of glutamine gluconeogenesis in kidney and liver and its alterations under pathological conditions are discussed. (+info)

The biochemical role of glutamine 188 in human galactose-1-phosphate uridyltransferase. (2/3706)

The substitution of arginine for glutamine at amino acid 188 (Q188R) ablates the function of human galactose-1-phosphate uridyltransferase (GALT) and is the most common mutation causing galactosemia in the white population. GALT catalyzes two consecutive reactions. The first reaction binds UDP-glucose (UDP-Glu), displaces glucose-1-phosphate (glu-1-P), and forms the UMP-GALT intermediate. In the second reaction, galactose-1-phosphate (gal-1-P) is bound, UDP-galactose (UDP-Gal) is released, and the free enzyme is recycled. In this study, we modeled glutamine, asparagine, and a common mutation arginine at amino acid 188 on the three-dimensional model of the Escherichia coli GALT-UMP protein crystal. We found that the amide group of the glutamine side chain could provide two hydrogen bonds to the phosphoryl oxygens of UMP with lengths of 2.52 and 2.82 A. Arginine and asparagine could provide only one hydrogen bond of 2. 52 and 3.02 A, respectively. To test this model, we purified recombinant human Gln188-, Arg188-, and Asn188-GALT and analyzed the first reaction in the absence of gal-1-P by quantitating glu-1-P released using enzyme-linked methods. Gln188-GALT displaced 80 +/- 7. 0 nmol glu-1-P/mg GALT/min in the first reaction. By contrast, both Arg188- and Asn188-GALT released more glu-1-P (170 +/- 8.0 and 129 +/- 28.4 nmol/mg GALT/min, respectively). The overall, double displacement reaction was quantitated in the presence of gal-1-P. Gln188-GALT produced 80,030 +/- 5,910 nmol glu-1-P/mg GALT/min, whereas the mutant Arg188- and Asn188-GALT released only 600 +/- 71. 2 and 2960 +/- 283.6 nmole glu-1-P/mg GALT/min, respectively. We conclude from these data that glutamine at position 188 stabilizes the UMP-GALT intermediate through hydrogen bonding and enables the double displacement of both glu-1-P and UDP-Gal. The substitution of arginine or asparagine at position 188 reduces hydrogen bonding and destabilizes UMP-GALT. The unstable UMP-GALT allows single displacement of glu-1-P with release of free GALT but impairs the subsequent binding of gal-1-P and displacement of UDP-Gal. (+info)

Kinetic impairment of nitrogen and muscle glutamine metabolisms in old glucocorticoid-treated rats. (3/3706)

Aged rats are more sensitive to injury, possibly through an impairment of nitrogen and glutamine (Gln) metabolisms mediated by glucocorticoids. We studied the metabolic kinetic response of adult and old rats during glucocorticoid treatment. The male Sprague-Dawley rats were 24 or 3 mo old. Both adult and old rats were divided into 7 groups. Groups labeled G3, G5, and G7 received, by intraperitoneal injection, 1.50 mg/kg of dexamethasone (Dex) for 3, 5, and 7 days, respectively. Groups labeled G3PF, G5PF, and G7PF were pair fed to the G3, G5, or G7 groups and were injected with an isovolumic solution of NaCl. One control group comprised healthy rats fed ad libitum. The response to aggression induced specifically by Dex (i.e., allowing for variations in pair-fed controls) appeared later in the aged rats (decrease in nitrogen balance from day 1 in adults but only from day 4 in old rats). The adult rats rapidly adapted to Dex treatment, whereas the catabolic state worsened until the end of treatment in the old rats. Gln homeostasis was not maintained in the aged rats; despite an early increase in muscular Gln synthetase activity, the Gln pool was depleted. These results suggest a kinetic impairment of both nitrogen and muscle Gln metabolisms in response to Dex with aging. (+info)

Paraoxonase 192 Gln/Arg gene polymorphism, coronary artery disease, and myocardial infarction in type 2 diabetes. (4/3706)

Paraoxonase is an HDL-associated enzyme implicated in the pathogenesis of atherosclerosis by protecting lipoproteins against peroxidation. Its biallelic gene polymorphism at codon 192 (glutamine/arginine) has been associated with coronary artery disease (CAD). To further evaluate the role of this paraoxonase gene polymorphism for CAD in type 2 diabetes, we determined the paraoxonase genotype in 288 type 2 diabetic patients (170 with and 118 without angiographically documented CAD). The paraoxonase 192 Gln/Arg genotype was assessed using polymerase chain reaction followed by AlwI digestion. The frequency of the Gln allele was 0.656 in the CAD patients and 0.746 in the controls (chi2 = 5.36, P = 0.02). Compared with the Gln/Gln genotypes, the age-adjusted odds ratio for CAD was 1.78 (95% CI 1.08-2.96, P = 0.02) in subjects carrying at least one Arg allele. In the multivariate analysis, this association was even stronger after correction for the possible confounders age, sex, smoking history, and hypertension. Among current and former smokers, the odds ratio (OR) for having CAD among patients with at least one Arg allele was 3.58 (1.45-9.53, P < 0.01). The paraoxonase Arg allele was not associated with the history of myocardial infarction (OR 1.20 [0.73-1.99, NS]), but was with the extent of CAD (OR for three-vessel disease 1.92 [1.15-3.27, P = 0.01]). Our data indicate that the 192 Arg allele of the human paraoxonase gene is a risk factor for CAD but not myocardial infarction in type 2 diabetic patients, a risk factor further modified by cigarette smoking. This risk could possibly be explained by a reduced ability of the paraoxonase Arg isoform to protect lipoproteins against peroxidation. (+info)

Analysis of zinc binding sites in protein crystal structures. (5/3706)

The geometrical properties of zinc binding sites in a dataset of high quality protein crystal structures deposited in the Protein Data Bank have been examined to identify important differences between zinc sites that are directly involved in catalysis and those that play a structural role. Coordination angles in the zinc primary coordination sphere are compared with ideal values for each coordination geometry, and zinc coordination distances are compared with those in small zinc complexes from the Cambridge Structural Database as a guide of expected trends. We find that distances and angles in the primary coordination sphere are in general close to the expected (or ideal) values. Deviations occur primarily for oxygen coordinating atoms and are found to be mainly due to H-bonding of the oxygen coordinating ligand to protein residues, bidentate binding arrangements, and multi-zinc sites. We find that H-bonding of oxygen containing residues (or water) to zinc bound histidines is almost universal in our dataset and defines the elec-His-Zn motif. Analysis of the stereochemistry shows that carboxyl elec-His-Zn motifs are geometrically rigid, while water elec-His-Zn motifs show the most geometrical variation. As catalytic motifs have a higher proportion of carboxyl elec atoms than structural motifs, they provide a more rigid framework for zinc binding. This is understood biologically, as a small distortion in the zinc position in an enzyme can have serious consequences on the enzymatic reaction. We also analyze the sequence pattern of the zinc ligands and residues that provide elecs, and identify conserved hydrophobic residues in the endopeptidases that also appear to contribute to stabilizing the catalytic zinc site. A zinc binding template in protein crystal structures is derived from these observations. (+info)

Deamidation of alpha-A crystallin from nuclei of cataractous and normal human lenses. (6/3706)

PURPOSE: To quantitate the extent of deamidation of asparagine-101, glutamine-50, and glutamine-6 of alpha-A crystallin in the nucleus from human cataractous and normal lenses. METHODS: Reverse phase chromatography was used to prepare alpha-A crystallin from total proteins of the nucleus from cataractous and age-matched normal human lenses. Synthetic peptides were made corresponding to the expected amidated and deamidated tryptic fragments containing asparagine-101, glutamine-50, and glutamine-6. The peptides were used to identify and quantitate amidated and deamidated forms of tryptic fragments from alpha-A crystallin eluting from a reverse phase column. RESULTS: Significant amounts of deamidation of asparagine-101 and glutamine-50, but not glutamine-6, were present in alpha-A crystallin from nuclear sections of both cataractous and age-matched normal lenses. Quantitative analysis of tryptic peptides containing these residues indicated no statistical difference in deamidation in cataractous versus normal lenses. CONCLUSIONS: There was no significant difference in the extent of deamidation of asparagine-101, glutamine-50, and glutamine-6 for alpha-A crystallin, purified from the nucleus of cataractous versus age-matched normal lenses. These results strongly suggest that deamidation of these residues does not play a role in the biogenesis of human nuclear cataract. (+info)

Subunit interface selectivity of the alpha-neurotoxins for the nicotinic acetylcholine receptor. (7/3706)

Peptide toxins selective for particular subunit interfaces of the nicotinic acetylcholine receptor have proven invaluable in assigning candidate residues located in the two binding sites and for determining probable orientations of the bound peptide. We report here on a short alpha-neurotoxin from Naja mossambica mossambica (NmmI) that, similar to other alpha-neurotoxins, binds with high affinity to alphagamma and alphadelta subunit interfaces (KD approximately 100 pM) but binds with markedly reduced affinity to the alphaepsilon interface (KD approximately 100 nM). By constructing chimeras composed of portions of the gamma and epsilon subunits and coexpressing them with wild type alpha, beta, and delta subunits in HEK 293 cells, we identify a region of the subunit sequence responsible for the difference in affinity. Within this region, gammaPro-175 and gammaGlu-176 confer high affinity, whereas Thr and Ala, found at homologous positions in epsilon, confer low affinity. To identify an interaction between gammaGlu-176 and residues in NmmI, we have examined cationic residues in the central loop of the toxin and measured binding of mutant toxin-receptor combinations. The data show strong pairwise interactions or coupling between gammaGlu-176 and Lys-27 of NmmI and progressively weaker interactions with Arg-33 and Arg-36 in loop II of this three-loop toxin. Thus, loop II of NmmI, and in particular the face of this loop closest to loop III, appears to come into close apposition with Glu-176 of the gamma subunit surface of the binding site interface. (+info)

Solution structure of the alpha-subunit of human chorionic gonadotropin. (8/3706)

The three-dimensional solution structure of the alpha-subunit in the alpha, beta heterodimeric human chorionic gonadotropin (hCG), deglycosylated with endo-beta-N-acetylglucosaminidase-B (dg-alpha hCG), was determined using 2D homonuclear and 2D heteronuclear 1H, 13C NMR spectroscopy at natural abundance in conjunction with the program package XPLOR. The distance geometry/simulated annealing protocol was modified to allow for the efficient modelling of the cystine knot motif present in alpha hCG. The protein structure was modelled with 620 interproton distance restraints and the GlcNAc residue linked to Asn78 was modelled with 30 protein-carbohydrate and 3 intraresidual NOEs. The solution structure of dg-alpha hCG is represented by an ensemble of 27 structures. In comparison to the crystal structure of the dimer, the solution structure of free dg-alpha hCG exhibits: (a) an increased structural disorder (residues 33-57); (b) a different backbone conformation near Val76 and Glu77; and (c) a larger flexibility. These differences are caused by the absence of the interactions with the beta-subunit. Consequently, in free dg-alpha hCG, compared to the intact dimer, the two hairpin loops 20-23 and 70-74 are arranged differently with respect to each other. The beta-GlcNAc(78) is tightly associated with the hydrophobic protein-core in between the beta-hairpins. This conclusion is based on the NOEs from the axial H1, H3, H5 atoms and the N-acetyl protons of beta-GlcNAc(78) to the protein-core. The hydrophobic protein-core between the beta-hairpins is thereby shielded from the solvent. (+info)

Causes of Hyperammonemia:

1. Liver disease or failure: The liver is responsible for filtering out ammonia, so if it is not functioning properly, ammonia levels can rise.
2. Urea cycle disorders: These are genetic conditions that affect the body's ability to break down protein and produce urea. As a result, ammonia can build up in the bloodstream.
3. Inborn errors of metabolism: Certain inherited disorders can lead to hyperammonemia by affecting the body's ability to process ammonia.
4. Sepsis: Severe infections can cause inflammation in the body, which can lead to hyperammonemia.
5. Kidney disease or failure: If the kidneys are not functioning properly, they may be unable to remove excess ammonia from the bloodstream, leading to hyperammonemia.

Symptoms of Hyperammonemia:

1. Lethargy and confusion
2. Seizures
3. Coma
4. Vomiting
5. Diarrhea
6. Decreased appetite
7. Weight loss
8. Fatigue
9. Headache
10. Nausea and vomiting

Diagnosis of Hyperammonemia:

1. Blood tests: Measurement of ammonia levels in the blood is the most common method used to diagnose hyperammonemia.
2. Urine tests: Measurement of urea levels in the urine can help determine if the body is able to produce and excrete urea normally.
3. Imaging tests: Imaging tests such as CT or MRI scans may be ordered to look for any underlying liver or kidney damage.
4. Genetic testing: If the cause of hyperammonemia is suspected to be a genetic disorder, genetic testing may be ordered to confirm the diagnosis.

Treatment of Hyperammonemia:

1. Dietary changes: A low-protein diet and avoiding high-aminogram foods can help reduce ammonia production in the body.
2. Medications: Medications such as sodium benzoate, sodium phenylbutyrate, and ribavirin may be used to reduce ammonia production or increase urea production.
3. Dialysis: In severe cases of hyperammonemia, dialysis may be necessary to remove excess ammonia from the blood.
4. Liver transplantation: In cases where the cause of hyperammonemia is liver disease, a liver transplant may be necessary.
5. Nutritional support: Providing adequate nutrition and hydration can help support the body's metabolic processes and prevent complications of hyperammonemia.

Complications of Hyperammonemia:

1. Brain damage: Prolonged elevated ammonia levels in the blood can cause brain damage, leading to cognitive impairment, seizures, and coma.
2. Respiratory failure: Severe hyperammonemia can lead to respiratory failure, which can be life-threatening.
3. Cardiac complications: Hyperammonemia can cause cardiac complications such as arrhythmias and heart failure.
4. Kidney damage: Prolonged elevated ammonia levels in the blood can cause kidney damage and failure.
5. Infections: People with hyperammonemia may be more susceptible to infections due to impaired immune function.

In conclusion, hyperammonemia is a serious condition that can have severe consequences if left untreated. It is essential to identify the underlying cause of hyperammonemia and provide appropriate treatment to prevent complications. Early detection and management of hyperammonemia can improve outcomes and reduce the risk of long-term sequelae.

... can exist in either of two enantiomeric forms, L-glutamine and D-glutamine. The L-form is found in nature. Glutamine ... Glutamine is synthesized by the enzyme glutamine synthetase from glutamate and ammonia. The most relevant glutamine-producing ... Glutamine is also released, in small amounts, by the lungs and brain. Although the liver is capable of relevant glutamine ... Glutamine is safe in adults and in preterm infants. Although glutamine is metabolized to glutamate and ammonia, both of which ...

https://en.wikipedia.org/wiki/Glutamine

... glutamine does not withstand sterilization procedures, whereas alanyl-glutamine does. Alanyl-glutamine's high solubility makes ... Alanyl-glutamine is a chemical compound which in the form L-alanyl-L-glutamine is used in dietary supplementation, in ... In cell culture, L-alanyl-L-glutamine is sometimes used as a replacement for L-glutamine because this dipeptide is stable in ... It is a dipeptide consisting of alanine and glutamine. As a dietary supplement, alanyl-glutamine protects the gastrointestinal ...

https://en.wikipedia.org/wiki/Alanyl-glutamine

... influences glutamine synthesis and glutamine hydrolysis. Glutamine is formed if an ammonium ion attacks the acyl-phosphate ... forming glutamine and inorganic phosphate. ADP and Pi do not dissociate until ammonia binds and glutamine is released. ATP ... Glutamine + ADP + phosphate Glutamine synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and ... "A glutamine riboswitch is a key element for the regulation of glutamine synthetase in cyanobacteria". Nucleic Acids Research. ...

https://en.wikipedia.org/wiki/Glutamine_synthetase

It was demonstrated that glnA RNAs correspond to glutamine-binding riboswitches, i.e., they sense glutamine concentrations in ... "A glutamine riboswitch is a key element for the regulation of glutamine synthetase in cyanobacteria". Nucleic Acids Res. doi: ... The glutamine riboswitch (formerly glnA RNA motif) is a conserved RNA structure that was predicted by bioinformatics. It is ... The fact that RNAs from both motifs selectively bind glutamine supports this hypothesis, but detailed structural data is not ...

https://en.wikipedia.org/wiki/Glutamine_riboswitch

... (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as ... In molecular biology, glutamine amidotransferases (GATase) are enzymes which catalyse the removal of the ammonia group from a ... Weng ML, Zalkin H (July 1987). "Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain". ... This activity is found in a range of biosynthetic enzymes, including glutamine amidotransferase, anthranilate synthase ...

https://en.wikipedia.org/wiki/Glutamine_amidotransferase

At GABAergic synapses, the cycle is called the GABA-glutamine cycle. Here the glutamine taken up by neurons is converted to ... Discoveries of glutamate and glutamine pools within intercellular compartments led to suggestions of the glutamate-glutamine ... Astrocytes readily convert glutamate to glutamine via the glutamine synthetase pathway and released into the extracellular ... The glutamate/GABA-glutamine cycle is a metabolic pathway that describes the release of either glutamate or GABA from neurons ...

https://en.wikipedia.org/wiki/Glutamate–glutamine_cycle

In enzymology, a protein-glutamine glutaminase (EC 3.5.1.44) is an enzyme that catalyzes the chemical reaction protein L- ... The systematic name of this enzyme class is protein-L-glutamine amidohydrolase. Other names in common use include ... Enzymes for selective deamidation of gamma-amide of peptide-bound glutamine". Biochemistry. 10 (7): 1222-9. doi:10.1021/ ... the two substrates of this enzyme are protein L-glutamine and H2O, whereas its two products are protein L-glutamate and NH3. ...

https://en.wikipedia.org/wiki/Protein-glutamine_glutaminase

This box: view edit Except where noted otherwise, data relate to Standard temperature and pressure. Reliability of data general note. ^a CID 738 from PubChem (Gln) ^a CID 145815 from PubChem (D) ^a CID 5961 from PubChem (L) (PubChem ID (CID) not in Wikidata, Chemical data pages, Chemical data pages cleanup ...

https://en.wikipedia.org/wiki/Glutamine_(data_page)

N-acyl-L-glutamine Thus, the two substrates of this enzyme are acyl-CoA and L-glutamine, whereas its two products are CoA and N ... In enzymology, a glutamine N-acyltransferase (EC 2.3.1.68) is an enzyme that catalyzes the chemical reaction acyl-CoA + L- ... The systematic name of this enzyme class is acyl-CoA:L-glutamine N-acyltransferase. Webster LT, Siddiqui UA, Lucas SV, Strong ... L-glutamine. This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other ...

https://en.wikipedia.org/wiki/Glutamine_N-acyltransferase

Other names in common use include glutamine transaminase K, and glutamine-phenylpyruvate aminotransferase. It employs one ... In enzymology, a glutamine-phenylpyruvate transaminase (EC 2.6.1.64) is an enzyme that catalyzes the chemical reaction L- ... Cooper AJ, Meister A (1974). "Isolation and properties of a new glutamine transaminase from rat kidney". J. Biol. Chem. 249 (8 ... Cooper AJ (1978). "Purification of soluble and mitochondrial glutamine transaminase K from rat kidney. Use of a sensitive assay ...

https://en.wikipedia.org/wiki/Glutamine—phenylpyruvate_transaminase

In enzymology, a glutamine-tRNA ligase (EC 6.1.1.18) is an enzyme that catalyzes the chemical reaction ATP + L-glutamine + ... glutamine-tRNA synthetase, glutamine translase, glutamate-tRNA ligase, glutaminyl ribonucleic acid, and GlnRS. This enzyme ... The systematic name of this enzyme class is L-glutamine:tRNAGln ligase (AMP-forming). Other names in common use include ... L-glutamine, and tRNA(Gln), whereas its 3 products are AMP, diphosphate, and L-glutaminyl-tRNA(Gln). This enzyme belongs to the ...

https://en.wikipedia.org/wiki/Glutamine—tRNA_ligase

In enzymology, a glutamine-pyruvate transaminase (EC 2.6.1.15) is an enzyme that catalyzes the chemical reaction L-glutamine + ... Other names in common use include glutaminase II, L-glutamine transaminase L, and glutamine-oxo-acid transaminase. This enzyme ... MEISTER A (1954). "Studies on the mechanism and specificity of the glutamine-alpha-keto acid transamination-deamidation ... Cooper JL, Meister A (1972). "Isolation and properties of highly purified glutamine transaminase". Biochemistry. 11 (5): 661-71 ...

https://en.wikipedia.org/wiki/Glutamine—pyruvate_transaminase

Other names in common use include glutamine phenylacetyltransferase, and phenylacetyl-CoA:L-glutamine N-acetyltransferase. This ... L-glutamine ⇌ {\displaystyle \rightleftharpoons } CoA + alpha-N-phenylacetyl-L-glutamine Thus, the two substrates of this ... In enzymology, a glutamine N-phenylacetyltransferase (EC 2.3.1.14) is an enzyme that catalyzes the chemical reaction ... The systematic name of this enzyme class is phenylacetyl-CoA:L-glutamine alpha-N-phenylacetyltransferase. ...

https://en.wikipedia.org/wiki/Glutamine_N-phenylacetyltransferase

L-glutamine-keto-scyllo-inositol aminotransferase, glutamine-scyllo-inosose transaminase, and L-glutamine-scyllo-inosose ... In enzymology, a glutamine-scyllo-inositol transaminase (EC 2.6.1.50) is an enzyme that catalyzes the chemical reaction L- ... The systematic name of this enzyme class is L-glutamine:2,4,6/3,5-pentahydroxycyclohexanone aminotransferase. Other names in ... the two substrates of this enzyme are L-glutamine and 2,4,6/3,5-pentahydroxycyclohexanone, whereas its two products are 2- ...

https://en.wikipedia.org/wiki/Glutamine—scyllo-inositol_transaminase

The substrates of this enzyme are ATP, deamido-NAD+, L-glutamine, and H2O, whereas its 4 products are AMP, diphosphate, NAD+, ... The systematic name of this enzyme class is deamido-NAD+:L-glutamine amido-ligase (AMP-forming). Bieganowski P, Pace HC, ... In enzymology, a NAD+ synthase (glutamine-hydrolysing) (EC 6.3.5.1) is an enzyme that catalyzes the chemical reaction ATP + ... Wojcik M, Seidle HF, Bieganowski P, Brenner C (November 2006). "Glutamine-dependent NAD+ synthetase. How a two-domain, three- ...

https://en.wikipedia.org/wiki/NAD _synthase_(glutamine-hydrolysing)

... (EC 6.3.5.4, asparagine synthetase (glutamine-hydrolysing), glutamine-dependent ... Asparagine+synthase+(glutamine-hydrolysing) at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: ... Tesson AR, Soper TS, Ciustea M, Richards NG (May 2003). "Revisiting the steady state kinetic mechanism of glutamine-dependent ... Boehlein SK, Richards NG, Schuster SM (March 1994). "Glutamine-dependent nitrogen transfer in Escherichia coli asparagine ...

https://en.wikipedia.org/wiki/Asparagine_synthase_(glutamine-hydrolysing)

The systematic name of this enzyme class is aspartyl-tRNAAsn:L-glutamine amido-ligase (ADP-forming). This enzyme participates ... In enzymology, an asparaginyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.6) is an enzyme that catalyzes the chemical ... and L-glutamine, whereas its 4 products are ADP, phosphate, asparaginyl-tRNA(Asn), and L-glutamate. This enzyme belongs to the ... family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. ...

https://en.wikipedia.org/wiki/Asparaginyl-tRNA_synthase_(glutamine-hydrolysing)

Glutamine amidotransferases). The systematic name of this enzyme class is adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido- ... In enzymology, an adenosylcobyric acid synthase (glutamine-hydrolysing) (EC 6.3.5.10) is an enzyme that catalyzes the chemical ... L-glutamine, and H2O; its four products are ADP, phosphate, adenosylcobyric acid, and L-glutamate. This enzyme belongs to the ... family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor ( ...

https://en.wikipedia.org/wiki/Adenosylcobyric_acid_synthase_(glutamine-hydrolysing)

The systematic name of this enzyme class is glutamyl-tRNAGln:L-glutamine amido-ligase (ADP-forming). This enzyme participates ... In enzymology, a glutaminyl-tRNA synthase (glutamine-hydrolysing) (EC 6.3.5.7) is an enzyme that catalyzes the chemical ... and L-glutamine, whereas its 4 products are ADP, phosphate, glutaminyl-tRNA(Gln), and L-glutamate. This enzyme belongs to the ... family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. ...

https://en.wikipedia.org/wiki/Glutaminyl-tRNA_synthase_(glutamine-hydrolysing)

In enzymology, a glutamine-fructose-6-phosphate transaminase (isomerizing) (EC 2.6.1.16) is an enzyme that catalyzes the ... The systematic name of this enzyme class is L-glutamine:D-fructose-6-phosphate isomerase (deaminating). This enzyme ... the two substrates of this enzyme are L-glutamine and D-fructose 6-phosphate, whereas its two products are L-glutamate and D- ... chemical reaction L-glutamine + D-fructose 6-phosphate ⇌ {\displaystyle \rightleftharpoons } L-glutamate + D-glucosamine 6- ...

https://en.wikipedia.org/wiki/Glutamine—fructose-6-phosphate_transaminase_(isomerizing)

Pyridoxal 5′-phosphate synthase (glutamine hydrolysing) (EC 4.3.3.6, PdxST) is an enzyme with systematic name D-ribose 5- ... Pyridoxal+5'-phosphate+synthase+(glutamine+hydrolyzing) at the US National Library of Medicine Medical Subject Headings (MeSH) ... This enzyme catalyses the following chemical reaction D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine ⇌ {\ ... L-glutamine + H2O ⇌ {\displaystyle \rightleftharpoons } L-glutamate + NH3 (1b) D-ribose 5-phosphate + D-glyceraldehyde 3- ...

https://en.wikipedia.org/wiki/Pyridoxal_5'-phosphate_synthase_(glutamine_hydrolyzing)

... is a protein that in humans is encoded by the SFPQ gene. GRCh38: Ensembl release 89 ... "Entrez Gene: Splicing factor proline and glutamine rich". Retrieved 2018-07-16. Peng R, Dye BT, Pérez I, Barnard DC, Thompson ...

https://en.wikipedia.org/wiki/Splicing_factor_proline_and_glutamine_rich

... is a protein that in humans is encoded by the QRSL1 gene. GRCh38: ... "Entrez Gene: Glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1". Retrieved 2018-05-17. Vieira AR, McHenry TG, Daack- ...

https://en.wikipedia.org/wiki/Glutaminyl-trna_synthase_(glutamine-hydrolyzing)-like_1

The systematic name of this enzyme class is hydrogenobyrinic-acid:L-glutamine amido-ligase (AMP-forming). This enzyme is also ... In enzymology, a hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) (EC 6.3.5.9) is an enzyme that catalyzes ... L-glutamine, and H2O; its four products are ADP, phosphate, hydrogenobyrinic acid a,c-diamide, and L-glutamate. This enzyme ... belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as ...

https://en.wikipedia.org/wiki/Hydrogenobyrinic_acid_a,c-diamide_synthase_(glutamine-hydrolysing)

... and glutamine". American Journal of Surgery. 183 (4): 471-9. doi:10.1016/s0002-9610(02)00823-1. PMID 11975938. "Glutamine". ... The amino acid glutamine has been used as a component of oral supplementation to reverse cachexia in people with advanced ... However, many of these clinical studies used HMB as a component of combination treatment with glutamine, arginine, leucine, ...

https://en.wikipedia.org/wiki/Cachexia

78: 3075-7. Yoshioka K, Takehara H, Okada A, Komi N (June 1992). "Glutamine antagonist with diet deficient in glutamine and ... Pinkus LM (1977). "Glutamine binding sites". Methods in Enzymology. 46: 414-27. doi:10.1016/S0076-6879(77)46049-X. ISBN 978-0- ... 683) and 244 nm (E1%1 cm 376). DON is used as inhibitor of different glutamine utilizing enzymes. Due to its similarity to ... 6-Diazo-5-oxo-L-norleucine (DON) is a glutamine antagonist, which was isolated originally from Streptomyces in a sample of ...

https://en.wikipedia.org/wiki/6-Diazo-5-oxo-L-norleucine

FTCD Glutamine deficiency, congenital; 610015; GLUL Glutaricaciduria, type I; 231670; GCDH Glutaricaciduria, type IIA; 231680; ...

https://en.wikipedia.org/wiki/List_of_OMIM_disorder_codes

... glutamine). These mutations and some key abnormalities they cause are: V205M: familial disease characterized by severe anemia ...

https://en.wikipedia.org/wiki/GATA1

Yoo HC, Yu YC, Sung Y, Han JM (2020). "Glutamine reliance in cell metabolism". Experimental & Molecular Medicine. 52 (9): 1496- ... Overexpression of SIRT4 inhibits cancer cell proliferation by inhibition of glutamine metabolism. GRCh38: Ensembl release 89: ...

https://en.wikipedia.org/wiki/Sirtuin_4

... (glutamine + -lysis) is a series of biochemical reactions by which the amino acid glutamine is lysed to ... Glutamine is the most abundant amino acid in the plasma and an additional energy source in tumor cells especially when ... Glutamine can be converted to citrate without NADH production, uncoupling NADH production from biosynthesis. Citric acid cycle ... High extracellular glutamine concentrations stimulate tumor growth and are essential for cell transformation. On the other hand ...

https://en.wikipedia.org/wiki/Glutaminolysis

Glutamine is one of the twenty amino acids generally present in animal proteins. The biochemical plays an important role in the ... Combined, glutamine and glutamic acid are responsible for the vast majority of the amino nitrogen located in the brain, and are ... Glutamine is one of the twenty amino acids generally present in animal proteins. A monoamide of glutamic acid, the biochemical ... Glutamine was not isolated as a component from a protein, however, until 1932 and was first chemically produced the following ...

https://micro.magnet.fsu.edu/aminoacids/pages/glutamine.html

Not All Glutamine Is Created Equal. Today, there are many choices available for Glutamine, but if you want to fuel your body ... Why Glutamine?. Glutamine is the most abundant amino acid in the human body. Though not considered and "essential" amino acid, ... There are 3 unique yet interwoven factors that can dramatically increase demand for glutamine within the human body; these ...

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L-glutamine: learn about side effects, dosage, special precautions, and more on MedlinePlus ... L-glutamine comes as a powder to be mixed with a liquid or soft wet food and taken by mouth twice a day. Take L-glutamine at ... Before taking L-glutamine,. *tell your doctor and pharmacist if you are allergic to L-glutamine, any other medications. ... Take L-glutamine exactly as directed. Do not take more or less of it or take it more often than prescribed by your doctor. ...

https://medlineplus.gov/druginfo/meds/a617035.html

L-Glutamine is helping HEAL my leaky gut. I take Glutagenics brand powdered L-glutamine which also has DGL and aloe in it and ... Youre confusing glutamine with glutamate.. As for where to get glutamine in your diet, you can find it in just about any ... where to buy L-glutamine). But does it really work?. YES. Within ten minutes of a dose of L-Glutamine, my sugar cravings ... You guys! L-glutamine is so cheap. I bought 120 500mg capsules of NOW Foods L-Glutamine for just $8.99! ...

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Protein target information for Glutamine--tRNA ligase (Escherichia coli CFT073). Find diseases associated with this biological ...

https://pubchem.ncbi.nlm.nih.gov/protein/Q8FJW4

glutamine from Neuroscience News features breaking science news from research labs, scientists and colleges around the world. ...

https://neurosciencenews.com/neuroscience-terms/glutamine/page/2/

Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)*Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) ... "Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)" is a descriptor in the National Library of Medicines controlled ... An enzyme that catalyzes the synthesis of fructose-6-phosphate plus GLUTAMINE from GLUTAMATE plus glucosamine-6-phosphate. ... This graph shows the total number of publications written about "Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)" by ...

https://connects.catalyst.harvard.edu/Profiles/display/Concept/Glutamine-Fructose-6-Phosphate%20Transaminase%20

Glutamine is the most abundant amino acid in the body. It plays a crucial role in cell volumizing and has powerful muscle ... Loading with glutamine may even increase the secretion of growth hormone. Studies show that supplementing with as little as two ... NutraBio L-Glutamine increases protein synthesis and growth hormone secretion, promotes nitrogen retention and muscle cell ... NutraBios free form L-Glutamine powder is absolutely pure glutamine manufactured by Ajinomoto. It is HPLC tested for purity ...

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Muscleblaze L-Glutamine, Muscleblaze Daily Multivitamin, Muscleblaze Pro One Gainer Xxxl and BODY SENSATION PURE L-GLUTAMINE ... L-glutamine Powder. Our range of products include Muscleblaze L-Glutamine, Muscleblaze Daily Multivitamin, Muscleblaze Pro One ... Muscleblaze L-Glutamine is the preferred choice of most athletes and bodybuilders because it takes your performance to the next ... Pure L-Glutamine is a product formulated for all fitness enthusiasts, gym professionals, and anyone with an active lifestyle, ...

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... suggesting that glutamine dependence may also be a feature of some human tumors. Glutamine starvation-induced cell death in ... and TRB3 in response to glutamine deprivation. Consistent with these findings, pharmacologic inhibition of glutamine metabolism ... Impact: Glutamine metabolism inhibitors or ATF4 agonists may be effective in MYC-overexpressing tumors. ... Clinical relevance: Glutamine metabolism genes are upregulated in MYCN-amplified human neuroblastomas. ...

https://aacrjournals.org/cancerdiscovery/article/3/1/OF25/3655/MYCN-Amplified-Neuroblastomas-Are-Glutamine

... utilize glutamine at high rates in addition to glucose (3,4). It was generally thought at that time that glutamine was only a ... Metabolic fate of glutamine in lymphocytes, macrophages and neutrophils. R. Curi1, P. Newsholme2, T.C. Pithon-Curi1, M. Pires- ... of the glutamine to glutamate, lactate and aspartate - Table 2). A high rate of glutamine utilization, but only partial ... absence of glutamine, lymphocytes do not proliferate in vitro; proliferation increases greatly with glutamine concentration (12 ...

https://indexmedicus.afro.who.int/iah/fulltext/BJMBR/v32_1/text2.htm

A Arginine B Citrulline C Glutamine D Glutamate E Lysine A 58 year old woman from PATH 132 at St. Georges University ...

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Effect of acidosis on glutamine transport by isolated rat renal brush-border and basolateral-membrane vesicles. ... Glutamine uptake was examined in isolated renal brush-border and basolateral-membrane vesicles from control and acidotic rats. ... Lowering the pH of the medium increased the initial rate of glutamine uptake in brush-border vesicles from acidotic, but not ... Effect of acidosis on glutamine transport by isolated rat renal brush-border and basolateral-membrane vesicles. Journal Article ...

https://scholars.duke.edu/display/pub701116

Glutamic acid is a precursor to the important inhibitory neurotransmitter GABA (gamma-aminobutyric acid). L-Glutamine also ... DescriptionL-Glutamine, a free-form amino acid, can be converted to glutamic acid. ... L-Glutamine, a free-form amino acid, can be converted to glutamic acid. Glutamic acid is a precursor to the important ... inhibitory neurotransmitter GABA (gamma-aminobutyric acid). L-Glutamine also plays an important role in ammonia disposal. ...

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An L-glutamine derivative in which one of the side-chain amide hydrogens of L-glutamine has been replaced by a phospho group. ...

https://zfin.org/action/ontology/term-detail/CHEBI:139506

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ʟ-⁠Glutamine is the most common naturally occurring amino acid found in muscle tissue, popul... Where can I buy L-Glutamine ( ... Glutamine is instrumental in muscle growth and repair following physical exertion. It also helps support immune and digestive ... Glutamine also decreases catabolism (the breakdown of muscle tissue), the process where glutamine leaves the muscle, causing ... ʟ-⁠Glutamine supplementation ensures that sufficient levels of glutamine are maintained within cells, minimizing dehydration ...

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Chez Nutri&Co, nous avons la conviction que lalimentation, la micronutrition, la Nutraceutique et lactivité physique permettent à chacun de prendre sa santé en main.. The information presented on this site is for information purposes only They are not a substitute for professional medical advice All rights reserved - Nutri&Co © 2023 ...

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Per4m Glutamine. £24.99. Quick View. Quick View. L-Glutamine is the most common amino acid found in muscle and is the primary ... Glutamine is the most abundant Amino Acid within muscle tissue, however when you train, Glutamine levels can be significantly ...

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Research and real-world evidence show that L-Glutamine supplementation during intense training cycles can help counter attack decreased intra-cellular glutamine levels, thereby helping maintain cell volume and hydration levels and provide an effective anti-catabloic (muscle preserving) nutritional strategy. (indiamart.com)
ʟ-⁠Glutamine supplementation ensures that sufficient levels of glutamine are maintained within cells, minimizing dehydration and catabolism. (newrootsherbal.com)
Supplementation prevents glutamine depletion in muscle cells after workouts. (newrootsherbal.com)
Glutamine supplementation helps replenish glutamine stores, which enhances the immune system, speeds recovery, and boosts muscle protein synthesis. (1stnutritions.com)
Supplementation with glutamine also helps to repair muscle cells after exercise. (peopletail.com)
Infection may improve with nutritional supplementation, particularly with regimens including zinc or glutamine. (medscape.com)

This makes ʟ-⁠glutamine conditionally essential in certain disease states to support the gut-barrier and immune function as well as overall protein use. (newrootsherbal.com)
Cabbage is high in glutamine - a conditionally essential amino acid which is an important fuel source for cells in our immune and gastrointestinal system. (wordpress.com)

Our range of products include Muscleblaze L-Glutamine, Muscleblaze Daily Multivitamin, Muscleblaze Pro One Gainer Xxxl, BODY SENSATION PURE L-GLUTAMINE and FULLY DOSED L-GLUTAMINE. (indiamart.com)
Pure L-Glutamine is a product formulated for all fitness enthusiasts, gym professionals, and anyone with an active lifestyle, wanting to improve their protein metabolism. (indiamart.com)

Glutamine is the most abundant amino acid in the human body. (vitacost.com)
MHP's Glutamine-SR 1000 provides a potent dosage of Glutamine, which is the most abundant amino acid in the body, and is used by your gut, immune system and muscles for fuel. (1stnutritions.com)
Glutamine is the most abundant Amino Acid within muscle tissue, however when you train, Glutamine levels can be significantly reduced as muscle tissue breaks down - even more so with the bodybuilding style of training. (stronggamers.com)
As the most abundant amino acid in the body, glutamine is required to maintain the health of rapidly dividing cells including immune and gastrointestinal cells. (peopletail.com)

Qing and colleagues showed that MYCN -amplified neuroblastoma cells were more sensitive to glutamine starvation than were nonamplified cells and that MYCN knockdown prevented cell death upon glutamine depletion. (aacrjournals.org)

ʟ-⁠Glutamine is the most common naturally occurring amino acid found in muscle tissue, populating in excess of 50% of skeletal muscle tissue. (newrootsherbal.com)
We analyzed skeletal muscle transcriptomics of critically ill patients , versus elective surgical controls, which revealed reduced expression of genes involved in mitochondrial metabolism and electron transport , with increases in glutathione cycling, glutamine , branched chain, and aromatic amino acid transport. (bvsalud.org)
meanwhile, the skeletal muscle and spleen were the only organs where glutamine 's contribution to the TCA cycle was significantly suppressed. (bvsalud.org)

Glutamine was not isolated as a component from a protein, however, until 1932 and was first chemically produced the following year. (fsu.edu)
AMP-activated protein kinase phosphorylates glutamine : fructose-6-phosphate amidotransferase 1 at Ser243 to modulate its enzymatic activity. (harvard.edu)
Glutamine and glucose are poorly oxidized by these cells and might produce important precursors for DNA, RNA, protein and lipid synthesis. (who.int)
GLUTAMINE-SR can also be added to your protein or meal replacement supplement. (1stnutritions.com)

Eric Newsholme's laboratory was the first to show glutamine utilization by lymphocytes and macrophages. (who.int)
The high rate of glutamine utilization and its importance in such cells have raised the question as to the source of this glutamine, which, according to current evidence, appears to be muscle. (who.int)
Only MHP has a Sustained Release Glutamine-SR which features a patented, sustained release technology to help support increased bio-availability and utilization of L-Glutamine. (1stnutritions.com)
To help improve glutamine absorption, MHP's Glutamine-SR features a patented, sustained release technology to help support increased bio-availability and utilization of L-Glutamine by providing a controlled steady supply so you can get the most of our your glutamine supplement. (1stnutritions.com)

In brush-border vesicles from acidotic animals, there was a significant increase in the initial rate of glutamine uptake compared with that in controls. (duke.edu)
Lowering the pH of the medium increased the initial rate of glutamine uptake in brush-border vesicles from acidotic, but not from control, rats. (duke.edu)

L-glutamine comes as a powder to be mixed with a liquid or soft wet food and taken by mouth twice a day. (medlineplus.gov)
Why use Applied Nutrition L-Glutamine Powder? (stronggamers.com)
L-Glutamine Vegan Amino Acid powder from CanPrev provides a high potency dose of pure, fermented L-glutamine in every scoop. (peopletail.com)

An enzyme that catalyzes the synthesis of fructose-6-phosphate plus GLUTAMINE from GLUTAMATE plus glucosamine-6-phosphate. (harvard.edu)
ʟ-⁠Glutamine is a precious precursor for glutathione synthesis, which serves as the body's most powerful antioxidant compound. (newrootsherbal.com)

NutraBio Glutamine is 100% pure, helping enhance muscle tissue repair and reduce soreness following workouts. (nutrabio.com)

Overexpression or amplification of MYC oncogenes rewires cellular metabolism and confers sensitivity to glutamine deprivation in vitro , but the mechanisms that underlie MYC-induced glutamine dependence are not well understood and the clinical relevance of these observations remains uncertain. (aacrjournals.org)

Though it is readily synthesized naturally within the body, glutamine is popularly sold as a nutritional supplement for athletes. (fsu.edu)
According to Dr. Ross, my body will have been weaned off sugar within a month, and I won't need to supplement with L-Glutamine any more. (foodrenegade.com)
No matter how intense or stressful activity you indulge in, Muscleblaze Glutamine Unflavoured supplement will help in the faster recovery and help you achieve a chiseled physique quickly. (indiamart.com)

ATF regulates MYC-mediated neuroblastoma cell death upon glutamine deprivation. (aacrjournals.org)
L-Glutamine regulates nitrogen transport to and from muscle tissue, thereby promoting amino acid balance. (vitaminlife.com)

NutraBio Glutamine is a potent cognitive enhancer that can keep your mind sharp and functioning optimally. (nutrabio.com)

Disappointing results from randomized controlled trials targeting glutamine and antioxidant metabolism in patients with sepsis have begged a deeper understanding of the tissue -specific metabolic response to sepsis . (bvsalud.org)

I bought 120 500mg capsules of NOW Foods L-Glutamine for just $8.99! (foodrenegade.com)

Glutamine metabolism genes are upregulated in MYCN -amplified human neuroblastomas. (aacrjournals.org)
Glutamine metabolism inhibitors or ATF4 agonists may be effective in MYC-overexpressing tumors. (aacrjournals.org)
Moreover, expression analysis of 80 primary neuroblastomas showed that multiple genes involved in glutamine metabolism were significantly upregulated in MYCN -amplified tumors compared with nonamplified tumors, suggesting that glutamine dependence may also be a feature of some human tumors. (aacrjournals.org)
Consistent with these findings, pharmacologic inhibition of glutamine metabolism or activation of ATF4 elicited a phenotype in MYCN -amplified cells similar to that caused by glutamine starvation and blocked tumor growth in vivo . (aacrjournals.org)
Tissue-specific reprogramming of glutamine metabolism maintains tolerance to sepsis. (bvsalud.org)

Plus, with its natural ability to boost immune function, glutamine can also help keep you feeling your best, both in and out of the gym. (nutrabio.com)

NutraBio L-Glutamine is vegetable based, naturally fermented 100% L-Glutamine manufactured right here in the United States! (nutrabio.com)

Combined, glutamine and glutamic acid are responsible for the vast majority of the amino nitrogen located in the brain, and are of central importance in the regulation of bodily ammonia levels. (fsu.edu)
L-Glutamine is the most common amino acid found in muscle and is the primary transporter of nitrogen into muscle cels. (stronggamers.com)

Whether you're looking to build lean muscle mass, improve your athletic performance, or recover faster after an intense workout, glutamine is the ticket. (nutrabio.com)

Glutamine is one of the twenty amino acids generally present in animal proteins. (fsu.edu)
L-glutamine is in a class of medications called amino acids. (medlineplus.gov)

This formulation provides Free Form L-Glutamine to promote optimal absorption and assimilation. (vitaminlife.com)
Glutamine-SR's patented sustained release technology allows for superior absorption and the continual feed of the critical amino acid glutamine. (1stnutritions.com)

Within ten minutes of a dose of L-Glutamine, my sugar cravings disappear. (foodrenegade.com)

By providing your muscles with this important amino acid, NutraBio Glutamine provides you with the crucial nutrient you need so that you'll be back in the gym in no time, pushing yourself harder and achieving the muscle growth you've been looking for. (nutrabio.com)
L-Glutamine on its own can be quickly broken down in your gut before it ever reaches your muscles. (1stnutritions.com)

Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)

Glutamine also decreases catabolism (the breakdown of muscle tissue), the process where glutamine leaves the muscle, causing muscle cells to become dehydrated. (newrootsherbal.com)

L-glutamine is used to is used to reduce the frequency of painful episodes (crises) in adults and children 5 years of age and older with sickle cell anemia (an inherited blood disorder in which the red blood cells are abnormally shaped [shaped like a sickle] and cannot bring enough oxygen to all parts of the body). (medlineplus.gov)
Knowledge of the metabolic fate of glutamine in these cells is important for the understanding of the role and function of this amino acid in the maintenance of the proliferative, phagocytic and secretory capacities of these cells. (who.int)
Indeed, it was not until the pioneering work of Eric Newsholme's laboratory in the 1980's that it was established that immune cells such as lymphocytes and macrophages could utilize glutamine at high rates in addition to glucose (3,4). (who.int)
It was generally thought at that time that glutamine was only a quantitatively important fuel for cells of the intestine and liver, and tumor cells (5). (who.int)
ATF4 activates proapoptotic genes upon glutamine deprivation in MYC-transformed cells. (aacrjournals.org)
Glutamine starvation-induced cell death in MYCN -amplified neuroblastoma cells was dependent on activating transcription factor 4 (ATF4), which directly increased expression of the proapoptotic genes PUMA , NOXA , and TRB3 in response to glutamine deprivation. (aacrjournals.org)
Furthermore, these drugs also induced PUMA / NOXA / TRB3 -dependent cell death and tumor inhibition in MYC-overexpressing Burkitt lymphoma cells, indicating that glutamine dependence may be a general feature of MYC-overexpressing tumors. (aacrjournals.org)
L-Glutamine is a major fuel source for intestinal, immune, and brain cells. (vitaminlife.com)

A recent study from our laboratory has shown that neutrophils also utilize glutamine at high rates (6). (who.int)
High intensity exercise and strict dieting can deplete glutamine concentrations. (1stnutritions.com)

NutraBio Glutamine helps amplify the production of neurotransmitters in your brain, helping enhance your memory, focus, and mental clarity. (nutrabio.com)

Studies have shown that supplementing with ʟ-⁠glutamine is effective in the replacement of these declining levels. (newrootsherbal.com)

Muscleblaze L-Glutamine is the preferred choice of most athletes and bodybuilders because it takes your performance to the next level when it comes to achieving maximum gains. (indiamart.com)

L-Glutamine also plays an important role in ammonia disposal. (ayurvedicherbsdirect.com)

L-Glutamine, a free-form amino acid, can be converted to glutamic acid. (ayurvedicherbsdirect.com)

A 100% pure form of fermented L-glutamine to help speed up muscle recovery, increase muscle growth, and maximize performance. (nutrabio.com)

Effect of acidosis on glutamine transport by isolated rat renal brush-border and basolateral-membrane vesicles. (duke.edu)
In brush-border vesicles from both groups of animals, two saturable transport systems mediated glutamine uptake. (duke.edu)
There was no difference in glutamine uptake by the two saturable transport systems in basolateral vesicles from control and acidotic animals. (duke.edu)
The data indicate that during acidosis there are alterations in glutamine transport by both the basolateral and brush-border membrane which could enhance its uptake by the renal-tubule cell for use in ammoniagenesis. (duke.edu)

We do not sell glutamine that is synthetic or made from human hair like much of the cheaper glutamine on the market. (nutrabio.com)

Glutamine is a powerful amino acid essential for muscle growth and recovery. (nutrabio.com)

Say goodbye to lackluster performance and hello to your new secret weapon - NutraBio Glutamine. (nutrabio.com)

Not only does glutamine improve your endurance and stamina. (nutrabio.com)

This graph shows the total number of publications written about "Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)" by people in Harvard Catalyst Profiles by year, and whether "Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)" was a major or minor topic of these publication. (harvard.edu)
On a procédé à la caractérisation isoenzymatique de ces isolats en utilisant 11 systèmes enzymatiques et comparé les résultats avec les profils enzymatiques des isolats originaux de L. major utilisés pour la leishmanisation. (who.int)

Adding glutamine can be the solution if you're looking to unlock untapped muscle growth and speed up muscle recovery. (nutrabio.com)

Anatomy1

Organisms1

Diseases1

Chemicals and Drugs43

Analytical, Diagnostic and Therapeutic Techniques and Equipment5

Phenomena and Processes6

Information Science3

Role of glutamine in human carbohydrate metabolism in kidney and other tissues. (1/3706)

The biochemical role of glutamine 188 in human galactose-1-phosphate uridyltransferase. (2/3706)

Kinetic impairment of nitrogen and muscle glutamine metabolisms in old glucocorticoid-treated rats. (3/3706)

Paraoxonase 192 Gln/Arg gene polymorphism, coronary artery disease, and myocardial infarction in type 2 diabetes. (4/3706)

Analysis of zinc binding sites in protein crystal structures. (5/3706)

Deamidation of alpha-A crystallin from nuclei of cataractous and normal human lenses. (6/3706)

Subunit interface selectivity of the alpha-neurotoxins for the nicotinic acetylcholine receptor. (7/3706)

Solution structure of the alpha-subunit of human chorionic gonadotropin. (8/3706)

Glutamine

Glutamate-Ammonia Ligase

Glutaminase

Ammonia

Methionine Sulfoximine

Diazooxonorleucine

Glutamates

Glutamic Acid

Amino Acids

Nitrogen

Glutamate Synthase

Nitrogen Isotopes

Ketoglutaric Acids

Glutamate Dehydrogenase

Amidophosphoribosyltransferase

Alanine

Nitrogenous Group Transferases

Aspartic Acid

Kinetics

Molecular Sequence Data

Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)

Amino Acid Sequence

Transaminases

Asparagine

Amino Acid Transport Systems, Neutral

Quaternary Ammonium Compounds

RNA, Transfer, Gln

Glucose

Escherichia coli

Azaserine

Citric Acid Cycle

Anthranilate Synthase

Hyperammonemia

Amino Acid Transport System ASC

Urea

Mutation

Ammonium Chloride

Ornithine

Arginine

Leucine

Carbon-Nitrogen Ligases

Parenteral Nutrition, Total

Enteral Nutrition

Magnetic Resonance Spectroscopy

Carbon Isotopes

Liver

Base Sequence

Biological Transport

Histidine Ammonia-Lyase

Citrulline

beta-Alanine

Amino Acid Transport System A

Transglutaminases

Mutagenesis, Site-Directed

Parenteral Nutrition

Aminooxyacetic Acid

PII Nitrogen Regulatory Proteins

Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)

Role of glutamine in human carbohydrate metabolism in kidney and other tissues. (1/3706)

The biochemical role of glutamine 188 in human galactose-1-phosphate uridyltransferase. (2/3706)

Kinetic impairment of nitrogen and muscle glutamine metabolisms in old glucocorticoid-treated rats. (3/3706)

Paraoxonase 192 Gln/Arg gene polymorphism, coronary artery disease, and myocardial infarction in type 2 diabetes. (4/3706)

Analysis of zinc binding sites in protein crystal structures. (5/3706)

Deamidation of alpha-A crystallin from nuclei of cataractous and normal human lenses. (6/3706)

Subunit interface selectivity of the alpha-neurotoxins for the nicotinic acetylcholine receptor. (7/3706)

Solution structure of the alpha-subunit of human chorionic gonadotropin. (8/3706)

Glutamine

Alanyl-glutamine

Glutamine synthetase

Glutamine riboswitch

Glutamine amidotransferase

Glutamate-glutamine cycle

Protein-glutamine glutaminase

Glutamine (data page)

Glutamine N-acyltransferase

Glutamine-phenylpyruvate transaminase

Glutamine-tRNA ligase

Glutamine-pyruvate transaminase

Glutamine N-phenylacetyltransferase

Glutamine-scyllo-inositol transaminase