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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.
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EC 2.1.1.376: glycine betaine—corrinoid protein Co-methyltransferase EC 2.1.1.377 : [methyl-Co(III) glycine betaine-specific corrinoid protein]—coenzyme M methyltransferase EC 2.1.1.378 : [methyl-Co(III) glycine betaine-specific corrinoid protein]—tetrahydrofolate methyltransferase
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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.
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.
Thus, the two substrates of this enzyme are S-adenosyl methionine and cytochrome c methionine, whereas its two products are S-adenosylhomocysteine and cytochrome c-S-methyl-methionine. This enzyme belongs to the family of transferases , specifically those transferring one-carbon group methyltransferases.