Threonine

L – Isomer is the only form involved in protein synthesis and is one of the 20 standard amino acids required for normal functioning in humans. It is considered an essential amino acid as it could be incorporated into the human body much faster than should be achieved through diet. Threonin is a hydrogen dispenser in enzymes that accompanies the production of hydrogen, which can be easily removed by using an enzyme such as the enzyme threonin in the synthesis of proteins. Sources: 4

In addition, the addition of threonine could reduce the growth suppression caused by excessive tryptophan and methionine. The metabolism of threonins consists in the fact that threonine can be converted into butyryl-CoENZyme by direct catalysis of the production of amino acids by the enzyme coenzyme C (co-oxidase). This amino acid is a gram that is regularly treated for the genetic spasticity disorder multiple sclerosis. Sources: 0, 4

Chickens usually absorb threonine in the duodenum, but it can also be a liver protein when taken up by crops, glandular stomachs or deposits in the bodySources: 0

However, it is still unclear how threonine is involved in the synthesis of proteins. Since only the amino acid concentrations were measured, the data did not allow speculations on amino acid flows. Sources: 0, 6

The transformation of threonine into glycine has been described as an important step in the synthesis of proteins and in the production of amino acids such as thion. Sources: 6

Increased levels of plasma threonine must therefore have an effect on the glycinergic neurotransmitter system in the brain. Other studies have also focused on several specific amino acids that can improve intestinal homeostasis by promoting healing and regeneration of the mucosa. There is evidence that the presence of glycine in blood plasma and other peripheral tissues, such as the pancreas, may indicate a positive effect of the amino acid in response to high glucose levels in the plasma compared to those in other peripheral elements and tissues. Sources: 2, 6

It is known, for example, that glutamine promotes induced inflammation by acting on NF – kB downregulation. Using a clear animal model for colitis, it was shown that a diet enriched with threonine, serine, proline and cysteine before and during the development of the disease restores mucus synthesis and stabilization of the intestinal microbiota. Similar findings were observed in mice with inflammatory bowel disease (IBD) and in people with Crohn’s disease. Sources: 2

In plant microorganisms, threonine synthesizes aspartic acid from partyl semialdehyde and homoserin and synthesizes it into particulate acid. Sources: 5

In contrast to other essential components of proteins, the role of threonine in the metabolism of mammals and humans is not defined. In bacteria, it is involved in the synthesis of aspartic acid and in the metabolism of amino acids and is involved in the production of amino acid glycolysis, the breakdown of carbohydrates and the formation of proteins. Sources: 5

Threonin is a hydrogen donor because hydrogen can be easily removed from the amino acid glycolysis of aspartic acid and in the synthesis of ketobutyrate and succinyl-COA. In addition, threonins can also be converted into alpha – ketOBUTyrates – and thus enter the pathway that leads to amber – CoA and thus to the formation of proteins. Sources: 5

Threonin is classified as an essential amino acid because it cannot be synthesized by the human body through chemical reactions from other compounds, nor can it be absorbed in food. L – Threonin isomer, the only form involved in protein synthesis, is required for normal functioning in humans. Sources: 5

The role of threonine in human metabolism is unclear, but the amino acid is needed as a building block for protein building blocks in the human body and for the production of proteins in animals. Sources: 3, 5

If the supply of one of these essential amino acids does not meet the requirements of an animal, it is considered to be limited. The essential amino acid cannot be synthesized by the animal and must therefore be supplied via foodSources: 3

In other words, to satisfy the needs of the body, it cannot be obtained if the horse or any other organism does not synthesize it. Sources: 1

L – Threonin is obtained by hydrolysis of proteins through pancreatic enzymes and digestion. When essential amino acids are sufficiently present, the horse’s body can convert the excess amino acid into carbon dioxide, which is exhaled and excreted as urea in the urine, and use it as an energy source. However, if the essential acid is deficient, it cannot be used by a horse or any other animal. Sources: 1

Threonine can be combined with the amino acid aspartic acid and methionine to help the liver, and with enough threonins in the body fat could be built up in this liver. Sources: 1

The effects of a lack of essential amino acids are generally non-specific, and many of the signs do not differ from the effect of partial or total calorie restriction. Sources: 1

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