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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.
A second pathway, which is usually restricted to liver and kidney in most mammals, involves betaine-homocysteine methyltransferase (BHMT) and requires trimethylglycine as a cofactor. [ 2 ] DNA processing and epigenetics
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.
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).
4524 17769 Ensembl ENSG00000177000 ENSMUSG00000029009 UniProt P42898 Q9WU20 RefSeq (mRNA) NM_005957 NM_001330358 NM_001161798 NM_010840 RefSeq (protein) NP_001317287 NP_005948 NP_001155270 NP_034970 Location (UCSC) Chr 1: 11.79 – 11.81 Mb Chr 4: 148.12 – 148.14 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Methylenetetrahydrofolate reductase (MTHFR) is the rate-limiting enzyme ...
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
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.