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|Section2={{Chembox Properties | C=6 | H=14 | N=4 | O=2 | Appearance = White crystals | Odor = Odourless | MeltingPtK = 533 | BoilingPtC = 368 | Solubility = 14.87 g/100 mL (20 °C) | SolubleOther = slightly soluble in ethanolinsoluble in ethyl ether | LogP = −1.652 | pKa = 12.488 | pKb = 1.509 }} |Section5={{Chembox Thermochemistry | DeltaHf = −624.9–−622.3 kJ mol−1 | DeltaHc = −3.7396–−3.7370 MJ mol−1 | Entropy = 250.6 J K−1 mol−1 | HeatCapacity = 232.8 J K−1 mol−1 (at 23.7 °C) }} |Section6={{Chembox Pharmacology | ATC_Supplemental = S }} |Section7={{Chembox Hazards | ExternalSDS = | GHSPictograms = | GHSSignalWord = WARNING | HPhrases = | PPhrases = | LD50 = 5110 mg/kg (rat, oral) }} |Section8={{Chembox Related | OtherFunction_label = alkanoic acids | OtherFunction = | OtherCompounds = }} |ImageFile1 = Arginine-3D-balls-by-AHRLS-2012.png}} Arginine (abbreviated as Arg or R) is an α- amino acid that is used in the biosynthesis of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. It contains an α- amino group, an α- carboxylic acid group, and a side chain consisting of a 3-carbon aliphatic straight chain ending in a guanidino group. At physiological pH, the carboxylic acid is deprotonated (−COO−), the amino group is protonated (−NH3+), and the guanidino group is also protonated to give the guanidinium form (-C-(NH2)2+), making arginine a charged, aliphatic amino acid. It is the precursor for the biosynthesis of nitric oxide. In humans, arginine is classified as a semiessential or conditionally essential amino acid, depending on the developmental stage and health status of the individual. Preterm infants are unable to synthesize or create arginine internally, making the amino acid nutritionally essential for them. Most healthy people do not need to supplement with arginine because it is a component of all protein-containing foods and can be synthesized in the body from glutamine via citrulline.


Arginine was first isolated from lupin and pumpkin seedlings by the German chemist Ernst Schulze and his assistant Ernst Steiger. They confirmed and published the structure in 1886.


Dietary sources

Arginine is a conditionally essential amino acid in humans and rodents, as it may be required depending on the health status or life cycle of the individual. For example, while healthy adults can supply their own requirement for arginine, immature and rapidly growing individuals require arginine in their diet, and it is also essential under physiological stress, for example during recovery from burns, injury and sepsis, or when the small intestine and kidneys, which are the major sites of arginine biosynthesis have been damaged. It is, however, an essential amino acid for birds, as they do not have a urea cycle. For some carnivores, for example cats, dogs and ferrets, arginine is essential, because after a meal, their highly efficient protein catabolism produces large quantities of ammonia which needs to be processed through the urea cycle, and if there is not enough arginine present, the resulting ammonia toxicity can be lethal. This is not a problem in practice, because meat contains sufficient arginine to avoid this situation. Animal sources of arginine include meat, dairy products and eggs, and plant sources include seeds of all types, for example grains, beans, and nuts.


Arginine is synthesized from citrulline in arginine and proline metabolism by the sequential action of the cytosolic enzymes argininosuccinate synthetase (ASS) and argininosuccinate lyase (ASL). This is an energetically costly process, because for each molecule of argininosuccinate that is synthesized, one molecule of adenosine triphosphate (ATP) is hydrolyzed to adenosine monophosphate (AMP), consuming two ATP equivalents. Citrulline can be derived from multiple sources: The pathways linking arginine, glutamine, and proline are bidirectional. Thus, the net utilization or production of these amino acids is highly dependent on cell type and developmental stage. On a whole-body basis, synthesis of arginine occurs principally via the intestinal–renal axis: the epithelial cells of the small intestine produce citrulline, primarily from glutamine and glutamate, which is carried in the bloodstream to the proximal tubule cells of the kidney, which extract citrulline from the circulation and convert it to arginine, which is returned to the circulation. This means that impaired small bowel or renal function can reduce arginine synthesis, increasing the dietary requirement. Synthesis of arginine from citrulline also occurs at a low level in many other cells, and cellular capacity for arginine synthesis can be markedly increased under circumstances that increase the production of inducible NOS ( iNOS). This allows citrulline, a byproduct of the NOS-catalyzed production of nitric oxide, to be recycled to arginine in a pathway known as the citrulline-NO or arginine-citrulline pathway. This is demonstrated by the fact that, in many cell types, NO synthesis can be supported to some extent by citrulline, and not just by by arginine. This recycling is not quantitative, however, because citrulline accumulates in NO-producing cells along with nitrate and nitrite, the stable end-products of NO breakdown.


Arginine plays an important role in cell division, wound healing, removing ammonia from the body, immune function, and the release of hormones. It is a precursor for the synthesis of nitric oxide (NO), making it important in the regulation of blood pressure.


Arginine's side chain is amphipathic, because at physiological pH it contains a positively charged guanidinium group, which is highly polar, at the end of a hydrophobic aliphatic hydrocarbon chain. Because globular proteins have hydrophobic interiors and hydrophilic surfaces, arginine is typically found on the outside of the protein, where the hydrophilic head group can interact with the polar environment, for example taking part in hydrogen bonding and salt bridges. For this reason, it is frequently found at the interface between two proteins. The aliphatic part of the side chain sometimes remains below the surface of the protein. Arginine residues in proteins can be deiminated by PAD enzymes to form citrulline, in a post-translational modification process called citrullination.This is important in fetal development, is part of the normal immune process, as well as the control of gene expression, but is also significant in autoimmune diseases.:275 Another post-translational modification of arginine involves methylation by protein methyltransferases.:176


Arginine is the immediate precursor of nitric oxide (NO), an important signaling molecule which can act as a second messenger as well as an intercellular messenger which regulates vasodilation, and also has functions in the immune system's reaction to infection. Arginine is also a precursor for urea, ornithine, and agmatine; is necessary for the synthesis of creatine; and can also be used for the synthesis of polyamines (mainly through ornithine and to a lesser degree through agmatine), citrulline, and glutamate. The presence of asymmetric dimethylarginine (ADMA), a close relative, inhibits the nitric oxide reaction; therefore, ADMA is considered a marker for vascular disease, just as L-arginine is considered a sign of a healthy endothelium.


L-arginine is generally recognized as safe (GRAS-status) at intakes of up to 20 grams per day.


The amino acid side-chain of arginine consists of a 3-carbon aliphatic straight chain, the distal end of which is capped by a guanidinium group, which has a pKa of 12.48, and is therefore always protonated and positively charged at physiological pH. Because of the conjugation between the double bond and the nitrogen lone pairs, the positive charge is delocalized, enabling the formation of multiple hydrogen bonds.


Growth hormone

Intravenously-administered arginine is used in growth hormone stimulation testsU.S. National Library of Medicine (September 2009 Growth hormone stimulation test because it stimulates the secretion of growth hormone. A review of clinical trials concluded that oral arginine increases growth hormone. However, a more recent trial reported that although oral arginine increased plasma levels of L-arginine it did not cause an increase in growth hormone.

High blood pressure

A meta-analysis showed that L-arginine reduces blood pressure with pooled estimates of 5.4 mmHg for systolic blood pressure and 2.7 mmHg for diastolic blood pressure. Supplementation with L-arginine reduces diastolic blood pressure and lengthens pregnancy for women with gestational hypertension, including women with high blood pressure as part of pre-eclampsia. It did not lower systolic blood pressure or improve weight at birth.

See also


External links

"green air" © 2007 - Ingo Malchow, Webdesign Neustrelitz
This article based upon the http://en.wikipedia.org/wiki/Arginine, the free encyclopaedia Wikipedia and is licensed under the GNU Free Documentation License.
Further informations available on the list of authors and history: http://en.wikipedia.org/w/index.php?title=Arginine&action=history
presented by: Ingo Malchow, Mirower Bogen 22, 17235 Neustrelitz, Germany