Nutrition Guide

S-Methylmethionine, or S-methyl-L-methionine, is a derivative of methionine with chemical formula C6H15NO2S. In plants, it is produced from methionine by the enzyme methionine S-methyltransferase.

S-Methylmethionine is sometimes called vitamin U in naturopathic medicine, but it is not recognized as a vitamin by mainstream nutrition science. Methionine in itself has not been demonstrated as effective for treating peptic and duodenal ulcers.[2][3][4] Its proponents claim that sources of methionine are limited, or claim it can be found only in raw cabbage; however, these claims are incorrect. Methionine is a common amino acid found in a wide variety of fruits, vegetables, and legumes.

Tyrosine is a starting material for neurotransmitters and increases plasma neurotransmitter levels (particularly dopamine and norepinephrine)[8] but has little if any effect on mood.[9][10][11] The effect on mood is more noticeable in humans subjected to stressful conditions (see below).

A number of studies have found tyrosine to be useful during conditions of stress, cold, fatigue,[12] prolonged work and sleep deprivation,[13][14] with reductions in stress hormone levels,[15] reductions in stress-induced weight loss seen in animal trials,[12] improvements in cognitive and physical performance[10][16][17] seen in human trials. Because tyrosine hydroxylase is the rate limiting enzyme, however, effects are less significant than those of l-dopa.

Tyrosine does not seem to have any significant effect on mood, cognitive or physical performance in normal circumstances.[18][19][20] A daily dosage supported in the literature is about 100 mg/kg for an adult.[21] The usual dosage amounts to 500-1500 mg per day (dose suggested by most manufacturers; usually an equivalent to 1-3 capsules of pure tyrosine). It is not recommended to exceed 12000 mg (12 g) per day. In fact, too high doses result in reduced levels of dopamine.[18] Tyrosine may decrease the absorption of other amino acids in high or chronic doses. It decreases absorption of l-dopa.

Three isomers of tyrosine are known. In addition to common amino acid L-tyrosine which is the para isomer (para-tyr, p-tyr or 4-hydroxyphenylalanine) there are two additional regioisomers, namely meta-tyrosine (m-tyr or 3-hydroxyphenylalanine or L-m-tyrosine) and ortho-tyrosine (o-tyr or 2-hydroxyphenylalanine) which occur in nature. The m-tyr and o-tyr isomers, which are rare, arise through non-enzymatic free-radical hydroxylation of phenylalanine under conditions of oxidative stress.[5][6]

m-Tyrosine and analogues (rare in nature and therefore available synthetically) have shown application in Parkinson’s Disease, Alzheimer’s disease and arthritis [7].

The decomposition of L-tyrosine (syn. para-hydroxyphenylalanine) begins with an ?-ketoglutarate dependent transamination through the tyrosine transaminase to para-hydroxyphenylpyruvate. The positional description para, abbreviated p, mean that the hydroxyl group and side chain on the phenyl ring are across from each other (see the illustration below).

The next oxidation step catalyzes by p-hydroxylphenylpyruvate-dioxygenase and splitting off CO2 homogentisate (2,5-dihydroxyphenyl-1-acetate). In order to split the aromatic ring of homogentisate, a further dioxygenase, homogentistate-oxygenase is required. Thereby, through the incorporation of a further O2 molecule, maleylacetoacetate is created.

Fumarylacetate is created maleylacetoacetate-cis-trans-isomerase through rotation of the carboxyl group created from the hydroxyl group via oxidation. This cis-trans-isomerase contains glutathione as a coenzyme. Fumarylacetoacetate is finally split via fumarylacetoacetate-hydrolase through the addition of a water molecule.

Thereby fumarate (also a metabolite of the citric acid cycle) and acetoacetate (3-ketobutyroate) are liberated. Acetoacetate is a ketone body, which is activated with succinyl-CoA, and thereafter it can be converted into acetyl-CoA which in turn can be oxidized by the citric acid cycle or be used for fatty acid synthesis.

Tyrosine is also the precursor to the pigment melanin.

In Papaver somniferum, the opium poppy, tyrosine is used to produce the alkaloid morphine.

In the adrenal gland, tyrosine is converted to levodopa by the enzyme tyrosine hydroxylase (TH). TH is also the rate-limiting enzyme involved in the synthesis of the catecholamine hormones dopamine, norepinephrine (noradrenaline), and epinephrine.

The thyroid hormones triiodothyronine (T3) and thyroxine (T4) in the colloid of the thyroid also are derived from tyrosine.

Some of the tyrosine residues can be tagged with a phosphate group (phosphorylated) by protein kinases. (In its phosphorylated state, it is referred to as phosphotyrosine). Tyrosine phosphorylation is considered to be one of the key steps in signal transduction and regulation of enzymatic activity. Phosphotyrosine can be detected through specific antibodies. Tyrosine residues may also be modified by the addition of a sulfate group, a process known as tyrosine sulfation.[4] Tyrosine sulfation is catalyzed by tyrosylprotein sulfotransferase (TPST). Like the phosphotyrosine antibodies mentioned above, antibodies have recently been described that specifically detect sulfotyrosine.

In plants and most microorganisms, tyr is produced via prephenate, an intermediate on the shikimate pathway. Prephenate is oxidatively decarboxylated with retention of the hydroxyl group to give p-hydroxyphenylpyruvate, which is transaminated using glutamate as the nitrogen source to give tyrosine and ?-ketoglutarate. Mammals synthesize tyrosine from the essential amino acid phenylalanine (phe), which is derived from food. The conversion of phe to tyr is catalyzed by the enzyme phenylalanine hydroxylase, a monooxygenase. This enzyme catalyzes the reaction causing the addition of an hydroxyl group to the end of the 6-carbon aromatic ring of phenylalanine, such that it becomes tyrosine.

Aside from being a proteogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. It occurs in proteins that are part of signal transduction processes. It functions as a receiver of phosphate groups that are transferred by way of protein kinases (so-called receptor tyrosine kinases). Phosphorylation of the hydroxyl group changes the activity of the target protein.

A tyrosine residue also plays an important role in photosynthesis. In chloroplasts (photosystem II), it acts as an electron donor in the reduction of oxidized chlorophyll. In this process, it undergoes deprotonation of its phenolic OH-group. This radical is subsequently reduced in the photosystem II by the four core manganese cluster.