Lysine is an essential amino acid found in protein-rich plant and animal foods and is involved in growth, tissue repair, collagen production, calcium absorption, antibody, hormone and enzyme production, and other important bodily functions. It has the effect of being a micronutrient, nutraceutical, anticonvulsant, E. coli metabolite, Saccharomyces cerevisiae metabolite, plant metabolite, human metabolite, algae metabolite, and animal metabolite.
Benefits of Lysine
Prevention of herpes simplex virus (HSV);
L-lysine is a natural antiviral and anti-disease agent that is known to protect against infection. It is known for reducing the severity and frequency of cold sores caused by the herpes simplex virus type 1. Lysine supplementation is beneficial for patients with recurrent infections due to herpes simplex virus (HSV). Arginine is required for herpes simplex virus replication. Lysine prevents HSV from using arginine, thus preventing the virus from multiplying. For this reason, taking high doses of supplemental lysine can help reduce the number of HSV lesions, such as cold sores and ulcers.
Reduces anxiety and other psychological symptoms and relieves stress;
Lysine is combined with B vitamins, magnesium, and omega-3 fatty acids to help reduce anxiety. Lysine, when combined with arginine, helps improve anxiety symptoms.
May improve symptoms of psychosis;
Prevents mouth sores and helps with **wounds;
Lysine is important for the formation of collagen, which contributes to the growth and maintenance of bones and connective tissue, including **. Collagen is able to help with mucosal wounds, which, like ulcers, affect the moist lining of the mouth. Taking lysine supplements can help boost collagen production, which in turn reduces and prevents ulcers and inflammation (mucositis) caused by radiation or chemotherapy, for example.
Lowers blood pressure;
Lysine is an effective natural remedy for high blood pressure. Lysine helps the kidneys filter out salt and water from the body, which naturally lowers blood pressure. In addition to this, it is important for lysine to produce carnitine in the body, which converts fatty acids into energy and lowers cholesterol levels.
Increases muscle strength;
Studies have shown that a diet rich in lysine prevents protein breakdown and improves muscle strength.
Osteoporosis
Lysine supplements can help the body absorb calcium, which is beneficial for osteoporosis.
Maintain a healthy gut;
L-lysine has an anti-inflammatory effect on the intestinal lining, and further research in this area will contribute to leaky gut syndrome. L-lysine has also been found to suppress pancreatitis, inflammation of the pancreas is another important part of the digestive system.
What is Lysine?
Lysine (Lysine) is an amino acid that is a precursor to many proteins. It contains a -amino group (protonated under biological conditions - NH3+ form), a -carboxylic acid group (deprotonated under biological conditions - COO-form), and a side-chain lysine ((CH2)4NH2), which is classified as an alkaline charged (at physiological pH) aliphatic amino acids. It is encoded by the codons AAA and AAG.
Molecular formula: C6H14N2O2.
Molecular weight: 14619
The chemical formula is: Ho2cch(NH2)(CH2)4NH2.
Chemical name: (2S)-2,6-diaminohexanoic acid (L-lysine).
The normal requirement for lysine** is about 8 grams or 12 milligrams per kilogram per day. Children and infants need more: children aged 11 to 12 years need 44 mg kg per day, and children aged 3 to 6 months need 97 mg kg per day. The best** from lysine comes from animal foods, but it's also found in some plant-based proteins.
Non-vegetarian foods of lysine** include: meat, chicken, dairy, eggs, fish.
Vegetarian lysine** includes: beans, wheat, germ, lentils, nuts, soybeans, spirulina.
The 10 foods with the highest lysine content are:
1.Lean beef and lean lamb — 3,582 mg per 100 grams.
2.Parmesan Cheese — 3,306 mg per 100 grams.
3.Turkey and chicken — 3,110 mg per 100 grams.
4.Pork — 2,757 mg per 100 grams.
5.Roasted soybeans — 2,634 mg 100 grams.
6.Tuna — 2,590 mg per 100 grams.
7.Shrimp — 2,172 mg per 100 grams.
8.Pumpkin seeds — 1,386 mg per 100 grams.
9.Eggs — 912 mg per 100 grams.
10.White beans — 668 mg 100 grams.
Biosynthesis of lysine
They are found in different organisms and use different enzymes and substrates to synthesize lysine. Lysine catabolism occurs through one of several pathways, the most common of which is the yeastine pathway.
Two pathways for the synthesis of lysine have been identified in nature. Aminoheptanetic acid (DAP) pathway and -aminoadipic acid (AAA) pathway.
DAP pathwayFound in both prokaryotes and plants, it begins with dihydropyridine dicarboxylic acid synthase (DHDPS) (EC4.).3.3.7) Catalytic condensation reaction between aspartic acid derivatization, L-aspartic acid semialdehyde and pyruvate to form (4 S)-4-hydroxy-2,3,4,5-tetrahydro-(2 S)-pyridine dicarboxylic acid (HTPA). NAD(P)H was then used as a proton donor, followed by dihydropyridine dicarboxylic acid reductase (DHDPR) (EC1.).3.1.26) Reduction product to give 2,3,4,5-tetrahydropyridine dicarboxylic acid (THDP). From this point onwards, four pathway variants have been identified, namely acetylase, aminotransferase, dehydrogenase, and succinylase pathway. Both the acetylase and succinylase mutation pathways use four enzyme-catalyzed steps, the aminotransferase pathway uses two enzymes, and the dehydrogenase pathway uses a single enzyme. These four mutation pathways converge to form the penultimate product, racemic-diaminoheptanetic acid, followed by diaminoheptanoic acid decarboxylase (DAPDC) (EC 4.).1.1.20) Enzymatic decarboxylation in catalyzed irreversible reactions to produce L-lysine. The DAP pathway is regulated at multiple levels, including upstream of the enzyme involved in aspartate processing and the initial DHDPS-catalyzed condensation step. Lysine creates a strong negative feedback loop for these enzymes, which subsequently regulates the entire pathway.
AAA pathwayInvolved-ketoglutarate and acetyl-CoA are condensed through the intermediate AAA to synthesize L-lysine. This pathway has been shown to be present in several yeast species as well as protists and higher fungi. Alternative variants of the AAA pathway have been reported in thermophilic Thermogenes and Pyrococcus Horikoshii, which may indicate that the pathway is more widespread in prokaryotes than originally proposed. The first and rate-limiting step in the AAA pathway is a condensation reaction between acetyl-CoA and -ketoglutarate, which is determined by homocitrate synthase (HCS) (EC2.).3.3.14) Catalytic generation of the intermediate homotype citrate CoA, which is hydrolyzed by the same enzyme to produce high citric acid. Homoaconitate is replaced by homoaconitase (HAC) (EC4.).2.1.36) Enzymatic dehydration to produce cis-homoaconitum. Then, HAC catalyzes a second reaction in which cis-homoacitic acid undergoes rehydration to produce high isocitrate. The resulting product is administered by high isocitrate dehydrogenase (HIDH) (EC11.1.87) Oxidative decarboxylation is performed to produce -ketoadipic acid. Glutamate is then used as an amino donor, through 5'- Pyridoxal phosphate (PLP)-dependent aminotransferase (PLP-AT) (EC2.)6.1.39) Formation of AAA. In fungi, AAA is administered by AAA reductase (EC12.1.95) reduction to -aminoadipic acid-semialdehyde, a unique process involving adenyylation and reduction activated by panthenylyl phosphate transferase (EC27.8.7)。Once semialdehyde is formed, saccharin reductase (EC15.1.10) Catalyze the condensation reaction with glutamate and NAD(P)H, as a proton donor, the imine is reduced to produce the penultimate product, saccharin. The final step of the fungal pathway involves saccharin dehydrogenase (SDH) (EC 1.).5.1.8) Catalyze the oxidative deamination of saccharin to produce L-lysine. In the variant AAA pathway found in some prokaryotes, AAA is first converted to N-acetyl-aminoadipic acid, which is phosphorylated and then reduced and dephosphorylated to -aldehyde. The aldehyde is then transferred by an amino group to N-acetyllysine, which is then deacetylated to give L-lysine.
Catabolism of lysine
Like all amino acids, the catabolism of lysine begins with the uptake of dietary lysine or the breakdown of intracellular proteins. Catabolism is also used as a means to control the concentration of free lysine within cells and maintain homeostasis to prevent the toxic effects of excess free lysine. Lysine catabolism involves a variety of pathways, but the most commonly used is the saccharin pathway, which occurs mainly in the liver (and equivalent organs) of animals, especially in the ** chondria. This is the opposite of the AAA pathway previously described.
In plants and animals, the first two steps of the saccharin pathway are catalyzed by a bifunctional enzyme, aminoadipic acid semialdehyde synthase (AASS), which has lysine-ketoglutarate reductase (LKR) (EC 15.1.8) ) and SDH activity, while in other organisms such as bacteria and fungi, both enzymes are encoded by different genes. The first step involves LKR catalyzing the reduction of L-lysine in the presence of -ketoglutarate to produce saccharin, with NAD(P)H as a proton donor. Saccharopine is then catalyzed by SDH in the presence of NAD+ to produce AAS and glutamate. AAS dehydrogenase (AASD) (EC 1.)2.1.31) The molecule is then further dehydrated to AAA. Subsequently, PLP-AT catalyzes a reverse reaction of the AAA biosynthesis pathway, resulting in the conversion of AAA to -ketoadipic acid. The product-ketoadipic acid is decarboxylated in the presence of NAD+ and coenzyme A to glutaryl-CoA, but the enzymes involved in it have not been fully elucidated.
Some evidence suggests that the 2-oxoadipate dehydrogenase complex (OADHC) is structurally homologous to the E1 subunit of the oxidized glutarate dehydrogenase complex (OGDHC) (EC12.4.2), responsible for decarboxylation reaction. Finally, glutaryl-CoA is passed by glutaryl-CoA dehydrogenase (EC13.8.6) Oxidative decarboxylation to crotonyl-CoA, which is then further processed through multiple enzymatic steps to produce acetyl-CoA;An essential carbon metabolite involved in the tricarboxylic acid cycle (TCA).
Normal lysine metabolism relies on many nutrients, including niacin, vitamin B6, riboflavin, vitamin C, glutamate, and iron.
Lysine and the gut microbe
The gut microbiome is another vital organ in the human body, and our body works with this microbiome every day, which actively interacts with the host to affect human health. Dysbiosis of the gut microbiosis has been linked to a variety of diseases, including obesity, diabetes, Crohn's disease (CD), cancer, and cardiovascular disease. Over the past few years, metaomics methods such as metagenomics, metatranscriptomics, and metaproteomics have been applied to study changes in the composition and function of the microbiome in patients with these diseases.
The body uses 22 different amino acid molecules to build more than 100,000 different types of proteins. Nine of these amino acid molecules are called "essential" amino acids because they must be extracted from our food or produced by the microbiome. The body doesn't just use proteins in the body like spare parts, but completely breaks them down into amino acid molecules in order to build new proteins. One of the key functions of the microbiome: lysine synthesis and metabolism.
Studies have shown that lysine plays an important role in stabilizing the three-dimensional structure of proteins, which is a very complex and critical aspect of the normal functioning of proteins in a healthy body. Dietary supplementation with lysine affects the absorption and metabolism of amino acids in the gut.
At the phylum level, lysine restriction increases the abundance of intestinal actinobacteria, saccharibacteria, and synergistetes. At the family level, the abundance of moraxellaceae, halomonadaceae, shewanellaceae, corynebacteriaceae, bacillaceae, comamonadaceae, microbacteriaceae, caulobacteraceae, synergistaceae increases with lysine restriction.
Lysine is an essential amino acid involved in many biological processes, including receptor affinity, protease cleavage points, endoplasmic reticulum retention, nuclear structure and function, muscle elasticity, and heavy metal chelation. Our understanding of the lysine regulation processes involved in the microbiome is still limited, and we will continue to update the scientific progress of gut microbiome and lysine as scientific research continues to develop.