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S-Methylmethionine (SMM) is a derivative of methionine with the chemical formula (CH 3) 2 S + CH 2 CH 2 CH (NH 3+)CO 2−. This cation is a naturally-occurring intermediate in many biosynthetic pathways owing to the sulfonium functional group. It is biosynthesized from L -methionine and S -adenosylmethionine by the enzyme methionine S ...
The methionine-derivative S-adenosylmethionine (SAM-e) is a cofactor that serves mainly as a methyl donor. SAM-e is composed of an adenosyl molecule (via 5′ carbon) attached to the sulfur of methionine, therefore making it a sulfonium cation (i.e., three substituents and positive charge).
S-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. Although these anabolic reactions occur throughout the body, most SAM is produced and consumed in the liver. [1]
These enzymatic reactions are found in many pathways and are implicated in genetic diseases, cancer, and metabolic diseases. Another type of methyl transfer is the radical S-Adenosyl methionine (SAM) which is the methylation of unactivated carbon atoms in primary metabolites, proteins, lipids, and RNA.
Methionine synthase (MS, MeSe, MTR) is primarily responsible for the regeneration of methionine from homocysteine in most individuals. In humans it is encoded by the MTR gene (5-methyltetrahydrofolate-homocysteine methyltransferase). [5][6] Methionine synthase forms part of the S-adenosylmethionine (SAMe) biosynthesis and regeneration cycle, [7 ...
AdoMet is a methyl donor for transmethylation. It gives away its methyl group and is also the propylamino donor in polyamine biosynthesis. S-adenosylmethionine synthesis can be considered the rate-limiting step of the methionine cycle. [2] As a methyl donor SAM allows DNA methylation.
Homocysteine (/ ˌ h oʊ m oʊ ˈ s ɪ s t iː n /) or Hcy: is a non-proteinogenic α-amino acid. It is a homologue of the amino acid cysteine, differing by an additional methylene bridge (-CH 2-). It is biosynthesized from methionine by the removal of its terminal C ε methyl group.
[36] [5] Choline and folate, interacting with vitamin B 12, act as methyl donors to homocysteine to form methionine, which can then go on to form SAM (S-adenosylmethionine). [5] SAM is the substrate for almost all methylation reactions in mammals.
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