|Jmol-3D images||Image 1|
|Molar mass||146.14 g mol−1|
|Melting point||185–186 °C decomp.|
|Solubility in water||soluble|
|Chiral rotation [α]D||+6.5º (H2O, c = 2)|
|Supplementary data page|
|n, εr, etc.|
Solid, liquid, gas
|Spectral data||UV, IR, NMR, MS|
| (verify) (what is: /?)
Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Glutamine (abbreviated as Gln or Q) is one of the 20 amino acids encoded by the standard genetic code. It is not recognized as anessential amino acid, but may become conditionally essential in certain situations, including intensive athletic training or certain gastrointestinal disorders. Its side-chain is an amide formed by replacing the side-chain hydroxyl of glutamic acid with anamine 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.
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
- Cellular energy, as a source, next to glucose
- Nitrogen donation for many anabolic processes, including the synthesis of purines
- Carbon donation, as a source, refilling the citric acid cycle
- Nontoxic transporter of ammonia in the blood circulation
Producing and consuming organs
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. 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.
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. In respect to the last point mentioned, different glutamine analogues, such as DON, Azaserine orAcivicin, are tested as anticancer drugs.
Examples for the usage of glutamine
In catabolic states of injury and illness, glutamine becomes conditionally essential (requiring intake from food or supplements). 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. In biological research, L-glutamine is commonly added to the media incell culture.  However, the high level of glutamine in the culture media may inhibit other amino acid transport activities. 
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.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.
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.