Endogenous Metabolite; mGluR

In addition to acting as a carbon source for cellular oxidation, L-glutamine peptide is a crucial precursor for the synthesis of proteins, amino acids, purine peptides, tandem peptides, and nucleotides. 0.7 mM of L-glutamine and 20 μM of L-glutamic acid are the body's most abundant extracellular forms of the amino acid [1]. After treating BRIN-BD11 cells with 10 mM L-glutamine for 24 hours in culture, 148 genes showed an increase in gene expression of more than 1.8 fold, while 18 genes showed a decrease in gene expression of more than 1.8 fold when compared with 1 mM. Many of these genes included those involved in signaling arousal, apoptosis, gene-regulated genes, and the island death response. The Ca2+-regulated phosphatases calcineurin and trypsin Pdx1 are activated more by L-glutamine [2].

L-Glutamine (Gln) is one of the 20 amino acids encoded by the standard genetic code. Its side chain is an amide; it is formed by replacing a side-chain hydroxyl of glutamic acid with an amine functional group. glutamine is found in foods high in proteins, such as fish, red meat, beans, and dairy products. glutamine is a supplement that is used in weightlifting, bodybuilding, endurance and other sports, as well as by those who suffer from muscular cramps or pain particularly elderly people. The main use of glutamine within the diet of either group is as a means of replenishing the body's stores of amino acids that have been used during exercise or everyday activities. Studies which are looking into problems with excessive consumption of glutamine thus far have proved inconclusive. However, normal supplementation is healthy mainly because glutamine is supposed to be supplemented after prolonged periods of exercise (for example, a workout or exercise in which amino acids are required for use) and replenishes amino acid stores; this being the main reason glutamine is recommended during fasting or for people who suffer from physical trauma, immune deficiencies, or cancer. There is a significant body of evidence that links glutamine-enriched diets with intestinal effects; aiding maintenance of gut barrier function, intestinal cell proliferation and differentiation, as well as generally reducing septic morbidity and the symptoms of Irritable Bowel Syndrome. The reason for such cleansing properties is thought to stem from the fact that the intestinal extraction rate of glutamine is higher than that for other amino acids, and is therefore thought to be the most viable option when attempting to alleviate conditions relating to the gastrointestinal tract. These conditions were discovered after comparing plasma concentration within the gut between glutamine-enriched and non glutamine-enriched diets. However, even though glutamine is thought to have cleansing properties and effects, it is unknown to what extent glutamine has clinical benefits, due to the varied concentrations of glutamine in varieties of food. It is also known that glutamine has various effects in reducing healing time after operations. Hospital waiting times after abdominal surgery are reduced by providing parenteral nutrition regimens containing amounts of glutamine to patients. Clinical trials have revealed that patients on supplementation regimes containing glutamine have improved nitrogen balances, generation of cysteinyl-leukotrienes from polymorphonuclear neutrophil granulocytes and improved lymphocyte recovery and intestinal permeability (in postoperative patients) - in comparison to those who had no glutamine within their dietary regime; all without any side-effects. 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.

We have investigated the effects of prolonged exposure (24 h) to the amino acid l-glutamine, on gene and protein expression using clonal BRIN-BD11 beta-cells. Expression profiling of BRIN-BD11 cells was performed using oligonucleotide microarray analysis. Culture for 24 h with 10 mM l-glutamine compared with 1 mM resulted in substantial changes in gene expression with 148 genes upregulated more than 1.8-fold, and 18 downregulated more than 1.8-fold, including many genes involved in cellular signaling, metabolism, gene regulation, and the insulin-secretory response. Subsequent functional experiments confirmed that l-glutamine increased the activity of the Ca(2+) regulated phosphatase calcineurin and the transcription factor Pdx1. Additionally, we demonstrated that beta-cell-derived l-glutamate was released into the extracellular medium at high rates. As calcineurin is a regulator of the glutamate N-methyl-d-aspartate (NMDA) receptor activity, we investigated the action of NMDA on nutrient-induced insulin secretion, and demonstrated suppressed insulin release. These observations indicate important long-term effects of l-glutamine in regulating beta-cell gene expression, signaling, and secretory function[1].

[1]. Mary Corless , et al. Glutamine Regulates Expression of Key Transcription Factor, Signal Transduction, Metabolic Gene, and Protein Expression in a Clonal Pancreatic Beta-Cell Line. J Endocrinol. 2006 Sep;190(3):719-27.
[2]. Newsholme P, et al. Glutamine and glutamate as vital metabolites. Braz J Med Biol Res. 2003 Feb;36(2):153-63. Epub 2003 Jan 29.[1].
[3]. Brosnan JT. Interorgan amino acid transport and its regulation. J Nutr. 2003 Jun;133(6 Suppl 1):2068S-2072S.
[4]. Newsholme P. Why is L-glutamine metabolism important to cells of the immune system in health, postinjury, surgery or infection? J Nutr. 2001 Sep;131(9 Suppl):2515S-22S; discussion 2523S-4S.

L-glutamine is an optically active form of glutamine having L-configuration. It has a role as an EC 1.14.13.39 (nitric oxide synthase) inhibitor, a nutraceutical, a micronutrient, a human metabolite, a Saccharomyces cerevisiae metabolite, an Escherichia coli metabolite and a mouse metabolite. It is a glutamine family amino acid, a proteinogenic amino acid, a glutamine and a L-alpha-amino acid. It is a conjugate base of a L-glutaminium. It is a conjugate acid of a L-glutaminate. It is an enantiomer of a D-glutamine. It is a tautomer of a L-glutamine zwitterion.

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Like other amino acids, glutamine is biochemically important as a constituent of proteins. Glutamine is also crucial in nitrogen metabolism. Ammonia (formed by nitrogen fixation) is assimilated into organic compounds by converting glutamic acid to glutamine. The enzyme which accomplishes this is called glutamine synthetase. Glutamine can then be used as a nitrogen donor in the biosynthesis of many compounds, including other amino acids, purines, and pyrimidines. L-glutamine improves nicotinamide adenine dinucleotide (NAD) redox potential.

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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 oral formulation of L-glutamine was approved by the FDA in July 2017 for use in sickle cell disease. This oral formulation is marketed under the tradename Endari by Emmaus Medical.

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L-Glutamine is a metabolite found in or produced by Escherichia coli (strain K12, MG1655). E. coli Metabolome Database (ECMDB) Glutamine is an Amino Acid. L-glutamine is an essential amino acid and precursor of major intracellular antioxidant molecules that is used in high doses to prevent vaso-occlusive crises in patients with sickle cell disease. L-glutamine has not been associated with serum enzyme elevations during therapy or to instances of idiosyncratic acute liver injury.

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Glutamine is a natural product found in Pinus densiflora, Trichoderma asperellum, and other organisms with data available. Glutamine is a nonessential amino acid. Glutamine can donate the ammonia on its side chain to the formation of urea (for eventual excretion by the kidneys) and to purines (necessary for the synthesis of nucleic acids). Glutamic acid-to-glutamine conversion, in which an ammonia group is added to glutamic acid (catalyzed by glutamine synthase), is of central importance in the regulation of toxic levels of ammonia in the body. This agent is a substrate for the production of both excitatory and inhibitory neurotransmitters (glutamate and GABA) and is also an important source of energy for the nervous system. Glutamine may become a conditionally essential amino acid during certain catabolic states.

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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.

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Used for nutritional supplementation, also for treating dietary shortage or imbalance. Used to reduce the acute complications of sickle cell disease in adult and pediatric patients 5 years of age and older. L-glutamine is an essential amino acid and precursor of major intracellular antioxidant molecules that is used in high doses to prevent vaso-occlusive crises in patients with sickle cell disease. L-glutamine has not been associated with serum enzyme elevations during therapy or to instances of idiosyncratic acute liver injury.

C5H10N2O3

146.14

146.0691

C, 41.09; H, 6.90; N, 19.17; O, 32.84

56-85-9

D-Glutamine;5959-95-5;DL-Glutamine;6899-04-3;L-Glutamine-15N;80143-57-3;L-Glutamine-13C5;184161-19-1;L-Glutamine-d5;14341-78-7;L-Glutamine-5-13C;159680-32-7;L-Glutamine-1-13C;159663-16-8;L-Glutamine-13C5,15N2;285978-14-5;L-Glutamine-15N2;204451-48-9;L-Glutamine-15N-1;59681-32-2;L-Glutamine-1,2-13C2;L-Glutamine-2-13C;180991-02-0;L-Glutamine-13C5,15N2,d5;2123439-02-9;L-Glutamine-15N2,d5

5961

Typically exists as white to off-white solids at room temperature

1.5±0.1 g/cm3

353.5±52.0 °C at 760 mmHg

185ºC

167.6±30.7 °C

0.0±1.8 mmHg at 25°C

1.564

-1.28

106.41

O([H])C([C@]([H])(C([H])([H])C([H])([H])C(N([H])[H])=O)N([H])[H])=O

ZDXPYRJPNDTMRX-VKHMYHEASA-N

InChI=1S/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10)/t3-/m0/s1

(2S)-2,5-diamino-5-oxopentanoic acid

Glavamin; Glumin; Glutamine; L-glutamine; glutamine; 56-85-9; Levoglutamide; L-(+)-Glutamine; Glutamic acid amide; Cebrogen; Stimulina;

2934.99.9001

Powder      -20°C    3 years

                     4°C     2 years

In solvent   -80°C    6 months

                  -20°C    1 month

Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)

H2O : ~33.33 mg/mL (~228.07 mM)

Solubility in Formulation 1: 7.69 mg/mL (52.62 mM) in PBS (add these co-solvents sequentially from left to right, and one by one), clear solution; with sonication (<60°C).

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 (Please use freshly prepared in vivo formulations for optimal results.)