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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.
In humans the enzyme's main purpose is to regenerate Met in the S-adenosylmethionine (SAM) cycle. The SAM cycle in a single turnover consumes Met and ATP and generates Hcy, and can involve any of a number of critical enzymatic reactions that use S-adenosylmethionine as the source of an active methyl group for methylation of nucleic acids ...
These enzymes use S-adenosylmethionine as a methyl donor and contain several highly conserved structural features between the three forms; these include the S-adenosylmethionine binding site, a vicinal proline-cysteine pair which forms a thiolate anion important for the reaction mechanism, and the cytosine substrate binding pocket.
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).
Dimethylglycine N-methyltransferase (EC 2.1.1.161, BsmB, DMT) is an enzyme with systematic name S-adenosyl-L-methionine:N,N-dimethylglycine N-methyltransferase (betaine-forming). [1] This enzyme catalyses the following chemical reaction
Another example of historical significance relating to transferase is the discovery of the mechanism of catecholamine breakdown by catechol-O-methyltransferase. This discovery was a large part of the reason for Julius Axelrod ’s 1970 Nobel Prize in Physiology or Medicine (shared with Sir Bernard Katz and Ulf von Euler ).
Levomefolic acid (INN, also known as L-5-MTHF, L-methylfolate and L-5-methyltetrahydrofolate and (6S)-5-methyltetrahydrofolate, and (6S)-5-MTHF) is the primary biologically active form of folate used at the cellular level for DNA reproduction, the cysteine cycle and the regulation of homocysteine.
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