![]() The safety and efficacy of L-glutamine oral powder were studied in a randomized trial of subjects ages five to 58 years old with sickle cell disease who had two or more painful crises within the 12 months prior to enrollment in the trial. Food and Drug Administration (FDA) approved L-glutamine oral powder, marketed as Endari, to reduce severe complications of sickle cell disease in people aged five years and older with the disorder. In states where tissue is being built or repaired, like growth of babies, or healing from wounds or severe illness, glutamine becomes conditionally essential. Humans obtain glutamine through catabolism of proteins in foods they eat. Glutamine is the most abundant naturally occurring, nonessential amino acid in the human body, and one of the few amino acids that can directly cross the blood–brain barrier. The most eager consumers of glutamine are the cells of intestines, the kidney cells for the acid-base balance, activated immune cells, and many cancer cells. Although the liver is capable of relevant glutamine synthesis, its role in glutamine metabolism is more regulatory than producing, since the liver takes up large amounts of glutamine derived from the gut. Glutamine is also released, in small amounts, by the lungs and brain. The most relevant glutamine-producing tissue is the muscle mass, accounting for about 90% of all glutamine synthesized. Glutamine is synthesized by the enzyme glutamine synthetase from glutamate and ammonia. 40 g/L in 2 days using glucose as a carbon source. Glutamine is produced industrially using mutants of Brevibacterium flavum, which gives ca. One of the most important functions of glutamine is its ability to be converted into α-KG, which helps to maintain the flow of the tricarboxylic acid cycle, generating ATPs. Glutamine also preserves nitrogen availability for synthesis of nucleotides and non-essential amino acids. Glutamine maintains redox balance by participating in glutathione synthesis and contributing to anabolic processes such as lipid synthesis by reductive carboxylation. For example, the inhibition of glutamine metabolism was reported to prevent growth of several tumors such as breast, liver, kidney and T-cell lymphoblastic leukemia. Studies have indicated the importance of glutamine in certain tumors. Glutamine level in the blood serum is the highest among other amino acids and is essential for many cellular functions. Ĭancer cells rely on glutamine metabolism as carbon and nitrogen sources. Integrity of healthy intestinal mucosa, though small randomized trials have shown no benefit in Crohn’s disease.Nontoxic transporter of ammonia in the blood circulation.Carbon donation, as a source, refilling the citric acid cycle.Nitrogen donation for many anabolic processes, including the synthesis of purines.Cellular energy, as a source, next to glucose.Regulation of acid-base balance in the kidney by producing ammonium.Lipid synthesis, especially by cancer cells.Protein synthesis, as any other of the 20 proteinogenic amino acids.Glutamine plays a role in a variety of biochemical functions: The dietary sources of glutamine include especially the protein-rich foods like beef, chicken, fish, dairy products, eggs, vegetables like beans, beets, cabbage, spinach, carrots, parsley, vegetable juices and also in wheat, papaya, Brussels sprouts, celery, kale and fermented foods like miso. In human blood, glutamine is the most abundant free amino acid. It is non-essential and conditionally essential in humans, meaning the body can usually synthesize sufficient amounts of it, but in some instances of stress, the body's demand for glutamine increases, and glutamine must be obtained from the diet. It is classified as a charge-neutral, polar amino acid. Its side chain is similar to that of glutamic acid, except the carboxylic acid group is replaced by an amide. Glutamine (symbol Gln or Q) is an α-amino acid that is used in the biosynthesis of proteins.
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