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In the field of enzymology, a betaine-homocysteine S-methyltransferase also known as betaine-homocysteine methyltransferase (BHMT) is a zinc metallo-enzyme that catalyzes the transfer of a methyl group from trimethylglycine and a hydrogen ion from homocysteine to produce dimethylglycine and methionine respectively: [2]
In enzymology, a homocysteine S-methyltransferase (EC 2.1.1.10) is an enzyme that catalyzes the chemical reaction. S-methylmethionine + L-homocysteine 2 L-methionine. Thus, the two substrates of this enzyme are S-methylmethionine and L-homocysteine, and it produces 2 molecules of L-methionine.
The island of Ireland's Food Safety Promotion Board uses The Food Pyramid, which is divided into five levels: bread, cereals and potatoes at the large base (6 or more servings); then fruit and vegetables (5); followed by milk, cheese and yogurt (3); then meat, fish, eggs and alternatives (2); and finally fats, high fat/sugar snacks, foods and ...
The S-methyl-L-cysteine residue irreversibly inactivates the protein, allowing only one transfer for each protein. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is DNA-6-O-methylguanine:[protein]-L-cysteine S-methyltransferase.
Sarcosine/dimethylglycine N-methyltransferase (EC 2.1.1.157, ApDMT, sarcosine-dimethylglycine methyltransferase, SDMT, sarcosine dimethylglycine N-methyltransferase, S-adenosyl-L-methionine:N,N-dimethylglycine N-methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:sarcosine(or N,N-dimethylglycine) N-methyltransferase (N,N-dimethylglycine(or betaine)-forming).
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 ] and is the enzyme responsible for linking the cycle to one-carbon metabolism via the folate cycle.
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S-adenosyl-L-methionine + DNA adenine S-adenosyl-L-homocysteine + DNA 6-methylaminopurine m6A was primarily found in prokaryotes until 2015 when it was also identified in some eukaryotes. m6A methyltransferases methylate the amino group in DNA at C-6 position specifically to prevent the host system to digest own genome through restriction enzymes.