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Ornithine is a non-proteinogenic α-amino acid that plays a role in the urea cycle. It is not incorporated into proteins during translation. Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency, a disorder of the urea cycle. The moiety derived from ornithine is called ornithyl.<ref name="Sivashanmugam2017">Template:Cite journal</ref>

Role in urea cycleEdit

L-Ornithine is one of the products of the action of the enzyme arginase on L-arginine, creating urea. Therefore, ornithine is a central component of the urea cycle, which enables the disposal of excess nitrogen. Ornithine itself is recycled and, in a sense, acts as a catalyst.

First, ammonia is converted into carbamoyl phosphate (Template:Chem) by carbamoyl phosphate synthetase. Ornithine transcarbamylase then catalyzes the reaction between carbamoyl phosphate and ornithine to form citrulline and phosphate (Pi). Another amino group is contributed by aspartate, leading to the formation of arginine and the byproduct fumarate. The resulting arginine, a guanidinium compound, is subsequently hydrolyzed by arginase to regenerate ornithine and release urea.

The two nitrogen atoms in urea are derived from ammonia and aspartate, while the nitrogen atoms in ornithine remain unchanged.

File:OTC reaction.png
Reaction mechanism:. The side-chain amino group of ornithine (Orn) nucleophilically attacks the carbonyl carbon of carbamoyl phosphate (CP), left, forming a tetrahedral transition state, middle. Charge rearrangement then releases citrulline (Cit) and phosphate (Pi), right.<ref name="pmid10747936">Template:Cite journal</ref>

Ornithine is not an amino acid directly coded for by DNA; that is, it is not a proteinogenic amino acid. However, in mammalian non-hepatic tissues, the primary role of the urea cycle is often the biosynthesis of arginine. As an intermediate in metabolic pathways, ornithine is thus quite important.<ref>Template:Cite journal</ref>

Other reactionsEdit

Ornithine, through the action of ornithine decarboxylase (EC 4.1.1.17), serves as the starting point for the synthesis of polyamines such as putrescine.

In bacteria such as E. coli, ornithine can be synthesized from L-glutamate.<ref>{{#invoke:citation/CS1|citation |CitationClass=web }}</ref>

File:Ornithine lactamization.svg
Ornithine lactamization

ResearchEdit

Exercise fatigueEdit

L-Ornithine supplementation has been shown to attenuate fatigue in subjects in placebo-controlled studies using a cycle ergometer. The results suggest that L-ornithine may exert an antifatigue effect by increasing the efficiency of energy consumption and promoting the excretion of ammonia.<ref>Template:Cite journal</ref><ref>Template:Cite journal</ref>

Weightlifting supplementEdit

Amino acid supplements, including L-ornithine, are frequently marketed to bodybuilders and weightlifters with claims of increasing levels of human growth hormone (HGH), muscle mass, and strength. A short, four-day clinical study conducted in 1993 reported that L-ornithine, in combination with L-arginine and L-lysine at 2 g/day each, did not increase HGH levels.<ref>Template:Cite journal</ref> A review published in 2002 concluded, "The use of specific amino acids to stimulate GH release by athletes is not recommended."<ref>Template:Cite journal</ref>

CirrhosisEdit

L-ornithine L-aspartate (LOLA), a stable salt of ornithine and aspartic acid, has been used in the treatment of cirrhosis<ref>Template:Cite journal</ref> and hepatic encephalopathy.<ref name="pmid30706425">Template:Cite journal</ref>

See alsoEdit

ReferencesEdit

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External linksEdit

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Template:Amino acid metabolism intermediates Template:Non-proteinogenic amino acids