User:Mamidi1

=Homoarginine= Homoarginine is an organic compound and amino acid derivative that through specific mechanisms, effects the cardiovascular system and potentially mortality. It is thought to increase nitric oxide supply and better endothelial functions.

Properties
Homoarginine, also known as L-Homoarginine, is an amino acid formed by lysine. It is accompanied by the molecular formula : C7H16N4O2. Homoarginine confers a molecular weight of 188.23.

Occurrences
Homoarginine is a nonprotein amino acid, also known as L-homoarginine. It growth inhibitor of Staphylococcus aureus, Escherichia Coli, as well as Candida albicans, thus it inhibits specific microbial growth and germination. It is assumed to be an antimetabolite of arginine. Many studies have shown that it acts as a competitive inhibitor in most cases, but there are also controversial studies showing that it is also an organ specific, non-competitive inhibitor as well. Studies have also shown that it is toxic when targeting Insecta and Rattus norvegicus. In it's inhibition, is also often found in occurrences with the lungs, cervix, testis and is an inhibitor of bone and liver-specific alkaline phosphohydrolases. Homoarginine is also found in occurrence with murine osteosarcoma cell proliferation.

It is also noted in studies that levels of L-Homoarginine increase during pregnancy, although more studies are under way for confirmation.

History
A cationic amino acid that is derived from lysine gives Homoarginine. History of this organic amino acid shows that Homoarginine could increase the availability of NO which is the basis to many of it's functions. It is shown that homoarginine on it's own acts as a precursor of NO. Also, it can by inhibit the enzyme arginase, which increases the intracellular concentration of the main substrate for NO synthase: L-arginine. Enzyme arginase is an enzyme which competes with NO synthase for L-arginine, the substrate in this situation. Historically researched, it is shown that there is not much significance of homoarginine to NO metabolism, however it is not completely understood. Yet, recent evidence suggests that homoarginine is positively related to endothelial function.

Homoarginine has further functions that correlate to cardiovascular health. Inhibition of platelet aggregation is an example. There are other examples of Homoarginine functions with inhibition of organ-specific activities as well. Homoarginine can also act as a stimulator, such as it's stimulation of insulin secretion.

Production
Homoarginine is formed as a derivative from lysine through reactions similar to those of the urea cycle. Just as in the urea cycle, during it's synthesis, ornithine is replaced by lysine. Ornithine-transcarbamoylase is the main enzyme for homoarginine synthesis. The production of homoarginine is based around the activity of this enzyme and therefore is specifically correlated to it. Although Ornithine-transcarbamoylase has a higher affinity to ornithine, it ends up catalyzing the transaminidation reaction of lysine as well. This is the key step that starts homoarginine production. The reason it also catalyzes this reaction with lysine is because of the low substrate selectivity in the reaction.

Another pathway for the production of Homoarginine includes glycine amidinotransferase (AGAT). This enzyme normally acts through the transfer of an amidino-group from arginine to glycine, resulting in formation of guanidino acetic acid, which is thus methylated by guanidinoacetate methyltransferase (GAMT) to form creatine. However, glycine amidinotransferase (AGAT) sometimes acts by using lysine instead of glycine in the reaction, therefore lysine becomes the acceptor of the amidino-group, resulting in the production of homoarginine.
 * ImageFile =Homoarginine Production.png|thumbnail|center|Homoarginine Production

Reactions
Homoarginine serves as a substrate for NO synthase. Also, homoarginine may inhibit arginase, which leads to an increase in availability of L-arginine for NO synthase to produce NO. Arginase is an enzyme that acts catalyzes the reaction of L-arginine and H2O to ornithine and urea. Thus, by inhibiting arginase, it can no longer catalyze this reaction and L-arginine and H2O won't be converted to ornithine and urea. This is homologous to the effects of Lysine itself on NO synthase as it also inhibits arginase. The reaction hypothesis for Homoarginine is supported by the correlation of homoarginine with an increased arginine-to-ornithine ratio. This therefore shows low arginase activity. It is also shown that although it can inhibit arginase activity, it is still not as good of an inhibitor of arginase than ornithine.

Uses
Homoarginine is used clinical studies, often with rats, to explore it's effects on cardiovascular health by acting as an inhibitor for organ-specific reactions. It is also used as a stimulator in some cases. Uses have shown to be limited mainly towards the studies of effects on the cardiovascular system.

A recent study was done to see if homoarginine deficiency is related to Sudden Cardiac Arrest in dialysis patients. Previous research had shown that homoarginine deficiency may lead to endothelial dysfunction due to decreased nitric oxide availability. The study was done with 1255 dibetic haemodialysis patients during a median of 4 years of follow up. Events seen during this study were SCD, stroke, myocardial infarction, and even death due to heart failure. Results led to the calculation that the risk of Sudden Cardiac Arrest increased three fold with every per unit decrease in homoarginine. This correlation was backing information for the hypothesis that there is a strong association with the presence of congestive heart failure and left ventricular hypertrophy with the presence of low homoarginine percentage. Results also showed a slight increased risk of stroke due to low levels of this amino acid derivative, yet no significance towards the effect on myocardial infarction.

L-Homoarginine is present in several plant species. Grass pea (Lathyrus sativus) is a very rich source. It is also present in traces in the common lentils ( Lens culiniaris) Since Homoarginine is a good substrate for Nitric oxide synthase the utility of these legumes, grass pea in particular, as a functional food for the cardiovasculature is a strong possibility. N/A

Safety
N/A