Methionine, sulfur-containing amino acid obtained by the hydrolysis of the majority of typical proteins. Initially separated from casein (1922 ), methionine accounts for about 5 percent of the weight of egg albumin; other proteins contain much smaller sized quantities of methionine. It is among numerous so-called necessary amino acids for mammals and fowl; i.e., they can not manufacture it. In bacteria it is manufactured from the amino acids cysteine and aspartic acid.

Methionine is essential in methylation (the procedure by which methyl, or -ch3, groups are added to substances) and is likewise a precursor of 2 other amino acids, cystine and cysteine. [1]

Other names

Methionine; methionine, l-; γ-methylthio-α-aminobutyric acid; butanoic acid, 2-amino-4-( methylthio)-, (s)-; cymethion; l-(-)- methionine; fulfilled; s-methionine; 2-amino-4-( methylthio) butyric acid; butyric acid, 2-amino-4-( methylthio)-; l(-)- amino-γ-methylthiobutyric acid; l-α-amino-γ-methylmercaptobutyric acid; l-γ-methylthio-α-aminobutyric acid; 2-amino-4-methylthiobutanoic acid; liquimeth; acimethin; l-2-amino-4-( methylthio) butyric acid; (s) -2- amino-4-( methylthio) butanoic acid; h-met-oh; l-homocysteine, s-methyl-; nsc 22946; 2-amino-4-methylthiobutanoic acid (s)-. [2]


Methionine is an amino acid. Amino acids are the building blocks that our bodies utilize to make proteins. Methionine is found in meat, fish, and dairy products. It plays a crucial role in the many functions within the body.

Methionine is typically taken by mouth to deal with liver conditions and viral infections along with many other uses. But there is minimal clinical research that supports these uses. [3]


L-methionine, the principal sulfur-containing amino acid in proteins, plays vital roles in cell physiology as an antioxidant and in the breakdown of fats and heavy metals. Previous studies suggesting making use of l-methionine as a treatment for anxiety and other illness suggest that it may likewise enhance memory and propose a function in brain function. Nevertheless, some evidence indicates that an excess of methionine can be damaging and can increase the threat of establishing type-2 diabetes, heart problem, particular types of cancer, brain alterations such as schizophrenia, and memory impairment. [4]


As an important amino acid, methionine is not synthesized de novo in human beings and other animals, which should ingest methionine or methionine-containing proteins. In plants and microbes, methionine biosynthesis comes from the aspartate family, together with threonine and lysine (through diaminopimelate, but not by means of α-aminoadipate). The primary backbone is originated from aspartic acid, while the sulfur may originate from cysteine, methanethiol, or hydrogen sulfide.

First, aspartic acid is transformed via β-aspartyl-semialdehyde into homoserine by two decrease actions of the terminal carboxyl group (homoserine has for that reason a γ-hydroxyl, for this reason the homo- series). The intermediate aspartate-semialdehyde is the branching point with the lysine biosynthetic path, where it is rather condensed with pyruvate. Homoserine is the branching point with the threonine path, where instead it is isomerised after triggering the terminal hydroxyl with phosphate (likewise utilized for methionine biosynthesis in plants).

Homoserine is then activated with a phosphate, succinyl or an acetyl group on the hydroxyl.

In plants and perhaps in some germs, phosphate is utilized. This action is shown threonine biosynthesis.

In the majority of organisms, an acetyl group is utilized to trigger the homoserine. This can be catalysed in germs by an enzyme encoded by metx or meta (not homologues). In enterobacteria and a restricted number of other organisms, succinate is used. The enzyme that catalyses the reaction is meta and the uniqueness for acetyl-coa and succinyl-coa is determined by a single residue. The physiological basis for the preference of acetyl-coa or succinyl-coa is unidentified, however such alternative routes exist in some other pathways (e.g. Lysine biosynthesis and arginine biosynthesis).

The hydroxyl activating group is then replaced with cysteine, methanethiol, or hydrogen sulfide. A replacement response is technically a γ-elimination followed by a version of a michael addition. All the enzymes included are homologues and members of the cys/met metabolism plp-dependent enzyme household, which is a subset of the plp-dependent fold type i clade. They use the cofactor plp (pyridoxal phosphate), which operates by stabilising carbanion intermediates.

If it reacts with cysteine, it produces cystathionine, which is cleaved to yield homocysteine. The enzymes included are cystathionine-γ-synthase (encoded by metb in germs) and cystathionine-β-lyase (metc). Cystathionine is bound differently in the two enzymes permitting β or γ reactions to take place. If it responds with complimentary hydrogen sulfide, it produces homocysteine. This is catalysed by o-acetylhomoserine aminocarboxypropyltransferase (formerly known as o-acetylhomoserine (thiol)- lyase. It is encoded by either mety or metz in bacteria. If it responds with methanethiol, it produces methionine straight. Methanethiol is a byproduct of catabolic path of certain compounds, for that reason this route is more unusual. If homocysteine is produced, the thiol group is methylated, yielding methionine. Two methionine synthases are known; one is cobalamin (vitamin b12) dependent and one is independent.

The path using cysteine is called the “transsulfuration path”, while the pathway using hydrogen sulfide (or methanethiol) is called “direct-sulfurylation path”.

Cysteine is likewise produced, particularly it can be made from a triggered serine and either from homocysteine (” reverse trans-sulfurylation path”) or from hydrogen sulfide (” direct sulfurylation path”); the activated serine is usually o-acetyl-serine (via cysk or cysm in e. Coli), however in aeropyrum pernix and some other archaea o-phosphoserine is utilized. Cysk and cysm are homologues, however come from the plp fold type iii clade. [5]

System of action

The mechanism of the possible anti-hepatotoxic activity of l-methionine is not completely clear. It is thought that metabolic process of high dosages of acetaminophen in the liver cause reduced levels of hepatic glutathione and increased oxidative tension. L-methionine is a precursor to l-cysteine. L-cysteine itself might have antioxidant activity. L-cysteine is likewise a precursor to the antioxidant glutathione. Antioxidant activity of l-methionine and metabolites of l-methionine appear to represent its possible anti-hepatotoxic activity. Recent research suggests that methionine itself has free-radical scavenging activity by virtue of its sulfur, as well as its chelating capability. [6]

Dietary sources

The met-content of proteins varies substantially depending upon the food source. Foods with a particularly high percentage consist of eggs (31 mg/g protein), cod (30 mg/g), and chicken (28 mg/g). Intermediate material is in beef (26 mg/g), pork (26 mg/g), milk (25 mg/g), and rice (24 mg/g). Grains and other plant-derived protein sources tend to include a lower percentage. Examples are corn (21 mg/g), wheat and oats (18 mg/g), rye and beans (15 mg/g), and cauliflower (14 mg/g). Cooking foods at high temperatures (browning) can reduce satisfied bioavailability due to oxidation (dworschak, 1980).

Because satisfied can not be manufactured in the body, appropriate quantities need to be supplied. Met and cys are carefully linked metabolically, and suggestions are frequently given for the amount of both sulfur amino acids (saa), for that reason. Healthy grownups need to get at least 13 mg/kg per day in mix. [7]

What is methionine used for?

The sulfur in methionine provides the body with many potential health advantages.

these might consist of:.

  • Nourishing the hair, skin, and nails
  • Securing the cells from pollutants
  • Helping with the detoxifying procedure
  • Slowing down the aging procedure
  • Aiding with the absorption of other nutrients (such as selenium and zinc)
  • Helping in the excretion of heavy metals (such as lead and mercury) assisting the body’s excretion process
  • Preventing excess fat buildup in the liver (by serving as a lipotropic representative– one that assists in the breakdown of fats)
  • Lowering cholesterol levels by increasing lecithin production in the liver

Tylenol (acetaminophen) overdose

Taking an oral (by mouth) dosage of methionine within 10 hours of tylenol (acetaminophen) overdose has been utilized in dealing with acetaminophen poisoning.2 methionine is believed to prevent the by-products of acetaminophen from damaging the liver as a result of an overdose of tylenol. Nevertheless, other treatments are likewise used and methionine might not be the most effective.


Although a few of the research study is combined regarding colon cancer and methionine, a 2013 meta-analysis reports, “this meta-analysis indicates that dietary methionine intake may be connected with reduced threat of colorectal cancer, especially colon cancer. More prospective studies with long follow-up time are required to confirm these findings.” for example, a 2016 research study reported “among the 10 important amino acids tested, methionine deprivation elicited the strongest repressive effects on the migration and invasion of these [breast] cancer cells.”.

Some studies show that a low methionine diet plan could be advantageous. There specify types of cancer cells that depend upon methionine to grow. Hence, limiting the intake of foods including methionine is useful for those who have some kinds of cancer, since it results in the death of the cancer cells.

Alzheimer’s disease

Research studies suggest that l-methionine might help to enhance memory and brain function, however according to a research study published by molecular neurodegeneration, “some proof suggests that an excess of methionine can be hazardous and can increase the danger of establishing type-2 diabetes, heart problem, certain types of cancer, brain modifications such as schizophrenia, and memory disability.”.

Research study on l-methionine and alzheimer’s disease has actually just been conducted in animal studies. In a 2015 mouse model study discovered that a diet plan enriched with l-methionine led to:.

  • An increase in amyloid (a substance that commonly develops in the brains of those with alzheimer’s illness)
  • An increase in the level of tau protein in the brain (an increase can lead to tau protein misfolding and clumping together to form unusual tau tangles, found in those with alzheimer’s)
  • An increase in oxidative tension and inflammatory action (both thought to raise the danger of alzheimer’s disease)
  • Memory disability and memory loss

The research study authors concluded, “taken together, the results of our research study indicate that an l-methionine-enriched diet plan triggers effects in [taking place in a living organism] and might contribute to the look of alzheimer’s- like illness in wild-type animals.”.

Other usages

Methionine is frequently considered other disorders, however there is a lack of medical research study results to support the security and effectiveness of its use in these conditions:.

  • Herpes simplex and herpes zoster (shingles)
  • Symptoms of menopause
  • Swelling of the pancreas
  • Liver problems
  • Anxiety
  • Alcohol addiction
  • Urinary tract infections (uti’s)
  • Asthma and allergic reactions
  • Schizophrenia [8]

It can produce molecules critical for normal cell function

Among the major functions of methionine in the body is that it can be utilized to produce other important molecules.

It is involved in the production of cysteine, the other sulfur-containing amino acid used to develop proteins in the body.

Cysteine can, in turn, produce a variety of particles, including proteins, glutathione and taurine.

Glutathione is in some cases called the “master anti-oxidant” due to its vital role in the defenses of your body.

It likewise plays a role in the metabolism of nutrients in the body and the production of dna and proteins.

Taurine has lots of functions that assist preserve the health and proper performance of your cells.

Among the most crucial particles methionine can be converted into is s-adenosylmethionine, or “sam”.

Sam takes part in many different chain reaction by moving part of itself to other molecules, consisting of dna and proteins.

Sam is also used in the production of creatine, an important particle for cellular energy.

Overall, methionine is straight or indirectly involved in lots of essential procedures in the body because of the particles it can end up being.

Methionine can convert into numerous sulfur-containing particles with essential functions, such as glutathione, taurine, sam and creatine. These molecules are important for the typical functions of the cells in your body.

It contributes in DNA methylation

Your dna consists of the info that makes you who you are.

While much of this details might stay the same for your entire life, ecological factors can actually change some elements of your dna.

This is one of the most fascinating functions of methionine– that it can convert into a particle called sam. Sam can alter your dna by adding a methyl group (a carbon atom and its attached hydrogen atoms) to it.

The quantity of methionine in your diet plan might impact how much of this process happens, but there are lots of unanswered questions about this.

It is possible that increasing methionine in the diet could either increase or decrease just how much your dna modifications as a result of sa.

In addition, if these changes happen, they could be beneficial sometimes however destructive in others.

For example, some research study has shown that diet plans higher in nutrients that add methyl groups to your dna might decrease risk of colorectal cancer.

However, other research has actually revealed that greater methionine intake might worsen conditions like schizophrenia, possibly due to adding more methyl groups to dna.

Among the particles produced by methionine, sam, can change your dna. It isn’t fully clear how the methionine material of your diet impacts this process, and it is possible that this procedure is beneficial sometimes and detrimental in others. [9]

Methionine metabolic process conditions

There are numerous conditions of methionine and sulfur metabolic process in addition to many other amino acid and organic acid metabolism conditions.

Homocysteine is an intermediate in methionine metabolic process; it is either remethylated to restore methionine or combined with serine in a series of transsulfuration responses to form cystathionine and after that cysteine. Cysteine is then metabolized to sulfite, taurine, and glutathione. Various problems in remethylation or transsulfuration can cause homocysteine to build up, leading to illness.

The primary step in methionine metabolic process is its conversion to adenosylmethionine; this conversion requires the enzyme methionine adenosyltransferase. Deficiency of this enzyme results in methionine elevation, which is not clinically substantial except that it causes false-positive neonatal screening results for homocystinuria.

Classic homocystinuria

This condition is caused by an autosomal recessive shortage of cystathionine beta-synthase, which catalyzes cystathionine development from homocysteine and serine. Homocysteine builds up and dimerizes to form the disulfide homocystine, which is excreted in the urine. Due to the fact that remethylation is intact, some of the extra homocysteine is converted to methionine, which builds up in the blood. Excess homocysteine inclines to thrombosis and has adverse results on connective tissue (perhaps including fibrillin), especially the eyes and skeleton; adverse neurologic impacts may be due to apoplexy or a direct impact.

Arterial and venous thromboembolic phenomena can take place at any age. Many clients develop ectopia lentis (lens subluxation), intellectual disability, and osteoporosis. Clients can have a marfanoid habitus even though they are not normally tall.

Medical diagnosis of classic homocystinuria is by neonatal screening for raised serum methionine; raised overall plasma homocysteine levels and/or dna testing are confirmatory. Enzymatic assay in skin fibroblasts can likewise be done.

Treatment of traditional homocystinuria is a low-methionine diet plan and l-cysteine supplements integrated with high-dose pyridoxine (a cystathionine synthetase cofactor) 100 to 500 mg orally once a day. Because about half of clients react to high-dose pyridoxine alone, some clinicians do not limit methionine intake in these patients. Betaine (trimethylglycine), which improves remethylation, can also help lower homocysteine. Betaine dose is typically started at 100 to 125 mg/kg orally 2 times a day and titrated based on homocysteine levels; requirements differ commonly, in some cases ≥ 9 g/day is needed. Folate 1 to 5 mg orally once a day is also given. With early treatment, intellectual outcome is typical or near typical. Vitamin c, 100 mg orally once a day, may also be provided to assist prevent thromboembolism.

Other kinds of homocystinuria

Different problems in the remethylation process can result in homocystinuria. Problems include deficiencies of methionine synthase (ms) and ms reductase (msr), delivery of methylcobalamin and adenosylcobalamin, and shortage of methylenetetrahydrofolate reductase (mthfr, which is required to generate the 5-methyltetrahydrofolate required for the ms response). Because there is no methionine elevation in these forms of homocystinuria, they are not identified by neonatal screening.

Clinical manifestations resemble other types of homocystinuria. In addition, ms and msr shortages are accompanied by neurologic deficits and megaloblastic anemia. Scientific manifestation of mthfr deficiency varies, consisting of intellectual special needs, psychosis, weak point, ataxia, and spasticity.

Diagnosis of ms and msr shortages is recommended by homocystinuria and megaloblastic anemia and validated by dna screening. Patients with cobalamin problems have megaloblastic anemia and methylmalonic acidemia. Mthfr deficiency is diagnosed by dna screening.

Treatment is by replacement of hydroxycobalamin 1 mg im once a day (for patients with ms, msr, and cobalamin problems) and folate in supplements similar to particular homocystinuria.


This condition is brought on by shortage of cystathionase, which transforms cystathionine to cysteine. Cystathionine build-up leads to increased urinary excretion but no medical signs.

Sulfite oxidase shortage

Sulfite oxidase transforms sulfite to sulfate in the last step of cysteine and methionine degradation; it requires a molybdenum cofactor. Deficiency of either the enzyme or the cofactor causes similar illness; inheritance for both is autosomal recessive.

In its most severe form, scientific manifestations appear in neonates and include seizures, hypotonia, and myoclonus, progressing to early death. Clients with milder forms may present similarly to cerebral palsy and may have choreiform motions.

Medical diagnosis of sulfite oxidase shortage is recommended by elevated urinary sulfite and validated by measuring enzyme levels in fibroblasts and cofactor levels in liver biopsy specimens and/or hereditary testing. Treatment of sulfite oxidase deficiency is encouraging. [10]


The following dosages have actually been studied in clinical research:.

By mouth

For acetaminophen (tylenol) poisoning: 2.5 grams of methionine every 4 hours for 4 doses to prevent liver damage and death. Methionine needs to be given within 10 hours of taking the acetaminophen. This need to be done by a healthcare expert. [11]

Methionine in the body

The estimated average requirement of adults for total sulphur amino acids (methionine and cysteine) is 15 mg per kg bodyweight and day (kg − 1d − 1). Suggestions for methionine consumption are confounded by enzyme cofactors and substrates such as vitamin b6, vitamin b9 (folate), vitamin b12, choline, betaine, and creatine. These nutrients make it possible for effective use of methionine– eg, they decrease the requirement for the body to transform methionine into cysteine. Therefore, although dietary methionine is essential for homoeostasis in grownups and for normal growth and advancement in children, dietary cysteine can lower the everyday methionine requirements.30 this result is often described as the sparing result of cysteine on methionine requirement., the obligatory minimum requirement for methionine consumption in grownups can be around 6 mg kg − 1d − 1.

The human body maintains a balance in between synthesis and deterioration of protein, and destruction of amino acids to get energy for the body’s requirements. In particular, the liver is necessary for the body’s protein turnover. The liver’s regulatory functions include the synthesis of non-essential amino acids, conversion of glucogenic amino acids to glucose or ketogenic amino acids to lipids, conversion of ammonia into urea, and the synthesis of most plasma proteins. A nutritionally appropriate diet plan can be ensured by consuming a vast array of protein (10– 35% of total energy intake for adults and 5– 10 % for kids). Protein consumption of 0 · 66 g kg − 1d − 1 of well balanced protein is sufficient for a typical adult. Typically, people have around 150 g protein per kg of bodyweight.35 whole-body protein turnover in humans is fairly rapid, with a typical protein synthesis rate estimated at around 4 g protein kg − 1d − 1 in the lack of net growth. The typical half-life of the total protein in human beings is most likely on the order of 80 days. We likewise assume that body methionine readily equilibrates for the most part with dietary intake, however long-lived proteins and tissues do exist. Assuming an uniform turnover of methionine with very first order kinetics, it would be anticipated that within 2 years more than 80% of methionine in the body is replenished with methionine used up from the diet (provided a methionine consumption or loss of 10 mg kg − 1d − 1, and a methionine swimming pool of 4 g/kg). [12]

Negative effects

To evaluate the body’s reactions to methionine, scientists will give a single big dosage of this amino acid and observe the results.

This dosage is far larger than the recommended consumption, typically around 45 mg/lb (100 mg/kg), or 6.8 grams for someone who weighs 150 pounds (68 kgs).

This kind of test has actually been carried out over 6,000 times, with mostly minor side effects. These minor adverse effects include lightheadedness, sleepiness and modifications in high blood pressure.

One major unfavorable event happened throughout among these tests, which resulted in the death of an individual with high blood pressure however health otherwise.

Nevertheless, it promises that an unexpected overdose of around 70 times the advised intake triggered the complications.

Overall, it appears that methionine is not particularly harmful in healthy human beings, other than at extremely high doses that would be virtually impossible to obtain through the diet plan.

Despite the fact that methionine is associated with the production of homocysteine, there is no evidence that consumption within a typical range threatens for heart health.


Individuals following lots of types of diet plans will often go beyond the suggested minimum consumption of methionine. Adverse effects in action to big dosages are often minor but might end up being dangerous at incredibly high dosages. [13]


Although methionine was labeled as being the most toxic amino acid in relation to development in animals, the evidence in people does not point to severe toxicity, other than at extremely high levels of consumption. Despite the function of methionine as a precursor of homocysteine, and the role of homocysteine in vascular damage and cardiovascular disease, there is no proof that dietary consumption of methionine within affordable limitations will trigger cardiovascular damage. A single dose of 100 mg/kg body weight has been revealed to be safe, however this dose is about 7 times the day-to-day requirement for sulfur amino acids, and duplicated intake for 1 wk was revealed to result in increased homocysteine levels. Daily dosages of 250 mg (i.e., 4 mg/kg daily) are only 25% of the daily requirement and have actually been revealed to be safe. Overall, the literature recommends that the single dosage which is usually given in the methionine loading test (100mg/kg/d) does not cause any serious complications, except in the extreme case when a 10-fold excess of methionine appears to have actually been given, and in clients who have schizophrenia or innate errors of sulfur amino acid metabolic process, such as hypermethioninemia. [14]


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