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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]
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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.
Trimethylglycine was the first betaine discovered; originally it was simply called betaine because it was discovered in sugar beets (Beta vulgaris subsp. vulgaris). [6] Several other betaines are now known.
Relevant enzymes include aspartokinase, aspartate-semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine O-transsuccinylase, cystathionine-γ-synthase, Cystathionine-β-lyase (in mammals, this step is performed by homocysteine methyltransferase or betaine—homocysteine S-methyltransferase.)
Homocysteine (/ ˌ h oʊ m oʊ ˈ s ɪ s t iː n /; symbol 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.
In enzymology, a thetin-homocysteine S-methyltransferase (EC 2.1.1.3) is an enzyme that catalyzes the chemical reaction dimethylsulfonioacetate + L-homocysteine ⇌ {\displaystyle \rightleftharpoons } S-methylthioglycolate + L-methionine
Betaine—homocysteine S-methyltransferase From an initialism : This is a redirect from an initialism to a related topic, such as the expansion of the initialism. Use {{ R from acronym }} instead for abbreviations that are pronounced as words, such as NATO and RADAR.