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Glutamine is genetically [[code for|coded for]] by the [[RNA]] [[codon]]s CAA and CAG. Glutamine's three-letter abbreviation is '''Gln''', and its one-letter abbreviation is '''Q'''. A three-letter designation for either glutamine or glutamic acid is '''Glx''' (one-letter abbreviation: '''Z'''). |
Glutamine is genetically [[code for|coded for]] by the [[RNA]] [[codon]]s CAA and CAG. Glutamine's three-letter abbreviation is '''Gln''', and its one-letter abbreviation is '''Q'''. A three-letter designation for either glutamine or glutamic acid is '''Glx''' (one-letter abbreviation: '''Z'''). |
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| − | Like other amino acids, glutamine is [[biochemistry|biochemically]] important as a constituent of [[protein]]s. Glutamine is also crucial in [[nitrogen]] [[metabolism]]. [[Ammonia]] (formed by [[nitrogen fixation]]) is assimilated into [[organic compound]]s by converting glutamic acid to glutamine. The [[enzyme]] that accomplishes this is called [[glutamine synthetase]]. Glutamine can, hence, be used as a nitrogen donor in the biosynthesis of many compounds, including other amino acids, [[purine]]s, and [[pyrimidine]]s. |
+ | Like other amino acids, glutamine is [[biochemistry|biochemically]] important as a constituent of [[protein]]s. Glutamine is also crucial in [[nitrogen]] [[metabolism]]. [[Ammonia]] (formed by [[nitrogen fixation]]) is assimilated into [[organic compound]]s by converting [[glutamic acid]] to glutamine. The [[enzyme]] that accomplishes this is called [[glutamine synthetase]]. Glutamine can, hence, be used as a nitrogen donor in the biosynthesis of many compounds, including other amino acids, [[purine]]s, and [[pyrimidine]]s. |
== Functions == |
== Functions == |
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  Chemical structure of L-glutamine | |
Glutamine | |
| Systematic (IUPAC) name | |
| (2S)-2-amino-4-carbamoyl-butanoic acid | |
| Identifiers | |
| CAS number | 56-85-9 |
| PubChem | 738 |
| Chemical data | |
| Formula | C5H10N2O3 |
| Mol. weight | 146.15 |
| Complete data | |
Glutamine (abbreviated as Gln or Q) is one of the 20 amino acids encoded by the standard genetic code. It is not recognized as an essential amino acid, but may become conditionally essential in certain situations, including intensive athletic training or certain gastrointestinal disorders.[citation needed] Its side-chain is an amide formed by replacing the side-chain hydroxyl of glutamic acid with an amine functional group, making it the amide of glutamic acid. Its codons are CAA and CAG. In human blood, glutamine is the most abundant free amino acid, with a concentration of about 500–900 µmol/l.[1]
Biochemistry
Formation and Nomenclature
Glutamine is genetically coded for by the RNA codons CAA and CAG. Glutamine's three-letter abbreviation is Gln, and its one-letter abbreviation is Q. A three-letter designation for either glutamine or glutamic acid is Glx (one-letter abbreviation: Z).
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 that accomplishes this is called glutamine synthetase. Glutamine can, hence, be used as a nitrogen donor in the biosynthesis of many compounds, including other amino acids, purines, and pyrimidines.
Functions
Glutamine plays a role in a variety of biochemical functions, including:
- Protein synthesis, as any other of the 20 proteinogenic amino acids
- Regulation of acid-base balance in the kidney by producing ammonium[2]
- Cellular energy, as a source, next to glucose[3]
- Nitrogen donation for many anabolic processes, including the synthesis of purines[1]
- Carbon donation, as a source, refilling the citric acid cycle[4]
- Nontoxic transporter of ammonia in the blood circulation
Producing and consuming organs
Producers
Glutamine is synthesized by the enzyme glutamine synthetase from glutamate and ammonia. The most relevant glutamine-producing tissue is the muscle mass, accounting for about 90% of all glutamine synthesized. Glutamine is also released, in small amounts, by the lung and the brain.[5] 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.[1]
Consumers
The most eager consumers of glutamine are the cells of intestines,[1] the kidney cells for the acid-base balance, activated immune cells,[6] and many cancer cells.[4] In respect to the last point mentioned, different glutamine analogues, such as DON, Azaserine or Acivicin, are tested as anticancer drugs.
Nutrition
Occurrences in nature
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.[7] In the body, it is found circulating in the blood, as well as stored in the skeletal muscles. It becomes conditionally essential (requiring intake from food or supplements) in states of illness or injury.[8]
Dietary sources
Dietary sources of L-glutamine include beef, chicken, fish, eggs, milk, dairy products, wheat, cabbage, beets, beans, spinach, and parsley. Small amounts of free L-glutamine are also found in vegetable juices.[8]
Uses
In catabolic states of injury and illness, glutamine becomes conditionally essential (requiring intake from food or supplements).[8] Glutamine has been studied extensively over the past 10–15 years, and has been shown to be useful in treatment of injuries, trauma, burns, and treatment-related side effects of cancer, as well as in wound healing for postoperative patients. Glutamine is also marketed as a supplement used for muscle growth in weightlifting, bodybuilding, endurance, and other sports. Evidence indicates glutamine, when orally loaded, may increase plasma HGH levels by stimulating the anterior pituitary gland.[9] In biological research, L-glutamine is commonly added to the media in cell culture.[10] [11] However, the high level of glutamine in the culture media may inhibit other amino acid transport activities. [12]
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 supply 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 supply; this being the main reason glutamine is recommended during fasting or for people who suffer from physical trauma, immune deficiencies, or cancer.[13]
Aiding gastrointestinal function
There have been several recent studies into the effects of glutamine and what properties it possesses, and, there is now 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. [1]
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. [1]
Aiding recovery after surgery
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. [3]
See also
- Bodybuilding supplements
- Dietitian
References
- ↑ 1.0 1.1 1.2 1.3 Brosnan JT (June 2003). Interorgan amino acid transport and its regulation. J. Nutr. 133 (6 Suppl 1): 2068S–2072S.
- ↑ Hall, John E.; Guyton, Arthur C. (2006). Textbook of medical physiology, 11th, St. Louis, Mo: Elsevier Saunders.
- ↑ DOI:10.1002/bies.20063
This citation will be automatically completed in the next few minutes. You can jump the queue or expand by hand - ↑ 4.0 4.1 DOI:10.1083/jcb.200703099
This citation will be automatically completed in the next few minutes. You can jump the queue or expand by hand - ↑ DOI:10.1590/S0100-879X2003000200002
This citation will be automatically completed in the next few minutes. You can jump the queue or expand by hand - ↑ PMID 11533304 (PMID 11533304)
Citation will be completed automatically in a few minutes. Jump the queue or expand by hand - ↑ PMID 9580550 (PMID 9580550)
Citation will be completed automatically in a few minutes. Jump the queue or expand by hand - ↑ 8.0 8.1 8.2 Glutamine. University of Maryland Medical Center. URL accessed on 2012-06-24.
- ↑ PMID 7733028 (PMID 7733028)
Citation will be completed automatically in a few minutes. Jump the queue or expand by hand - ↑ Thilly, William G. (1986). Mammalian cell technology, London: Butterworths. URL accessed 2012-06-22. "13 amino acids in Eagle's popular culture medium...are arginine, cyst(e)ine, glutamine..."
- ↑ Yang H, Roth CM, Ierapetritou MG. (2011) Analysis of amino acid supplementation effects on hepatocyte cultures using flux balance analysis, OMICS, A Journal of Integrative Biology, 15(7-8): 449–460.
- ↑ Yang H, Ierapetritou MG, Roth CM. (2010) Effects of amino acid transport limitations on cultured hepatocytes, Biophysical Chemstry, 152(1-3):89-98.
- ↑ Glutamine used for the Immune System and Cancer. URL accessed on 2006-07-28.
bBoza J.J., Dangin M., Moennoz D., Montigon F., Vuichoud J., Jarret A., Pouteau E., Gremaud G., Oguey-Araymon S., Courtois D., Woupeyi A., Finot P.A. and Ballevre O. Free and protein-bound glutamine have identical splanchnic extraction in healthy human volunteers. Am J Physiol Gastrointest Liver Physiol. 2001 Jul; 281(1): G267-74. PMID 11408280 Free text
McAnena O.J., Moore F.A., Moore E.E., Jones T.N. and Parsons P. Selective uptake of glutamine in the gastrointestinal tract: confirmation in a human study. Br J Surg. 1991 Apr; 78(4): 480-2. PMID 1903318
Morlion B.J., Stehle P., Wachtler P., Siedhoff H.P., Koller M., Konig W., Furst P., Puchstein C. Total parenteral nutrition with glutamine dipeptide after major abdominal surgery. Ann Surg. 1998 Feb; 227(2): 302-8. PMID 9488531
Jiang Z.M., Cao J.D., Zhu X.G., Zhao W.X., Yu J.C., Ma E.L., Wang X.R., Zhu M.W., Shu H., Liu Y.W. The impact of alanyl-glutamine on clinical safety, nitrogen balance, intestinal permeability, and clinical outcome in postoperative patients: a randomised, double-blind, controlled study of 120 patients. JPEN J Parenter Enteral Nutr. 1999 Sep-Oct;23(5 Suppl):S62-6. PMID 10483898
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