PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22093367-2 2012 This activity is compromised when vitamin B12 concentration is low because methionine synthase activity is reduced, lowering the concentration of S-adenosyl methionine (SAM) which in turn may diminish DNA methylation and cause folate to become unavailable for the conversion of dUMP to dTMP. S-Adenosylmethionine 146-167 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 75-94 26989453-4 2016 MS activity was dependent upon methylcobalamin (MeCbl) or the combination of hydroxocobalamin (OHCbl) and S-adenosylmethionine (SAM). S-Adenosylmethionine 106-126 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 0-2 26989453-4 2016 MS activity was dependent upon methylcobalamin (MeCbl) or the combination of hydroxocobalamin (OHCbl) and S-adenosylmethionine (SAM). S-Adenosylmethionine 128-131 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 0-2 24352086-1 2013 Vitamin B12 is a cofactor of methionine synthase in the synthesis of methionine, the precursor of the universal methyl donor S-Adenosylmethionine (SAMe), which is involved in different epigenomic regulatory mechanisms and especially in brain development. S-Adenosylmethionine 125-145 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 29-48 23032700-2 2013 Cobalamin is the cofactor of methionine synthase, a key enzyme of the methionine cycle which synthesizes methionine, the precursor of cell S-adenosyl-methionine synthesis. S-Adenosylmethionine 141-160 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 29-48 23579332-6 2013 The ratio of the methyl donor S-adenosylmethionine to the methylation inhibitor S-adenosylhomocysteine was decreased, in association with an increase in HCY and a global decrease in DNA methylation, indicative of decreased activity of the redox-sensitive enzyme methionine synthase. S-Adenosylmethionine 30-50 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 262-281 24101362-2 2013 Genes encoding enzymes for methylenetetrahydrofolate reductase (MTHFR) and methionine synthase (MTR) may determine biomarkers of the cycle including homocysteine (HCY), S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH). S-Adenosylmethionine 169-189 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 75-94 24101362-2 2013 Genes encoding enzymes for methylenetetrahydrofolate reductase (MTHFR) and methionine synthase (MTR) may determine biomarkers of the cycle including homocysteine (HCY), S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH). S-Adenosylmethionine 191-194 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 75-94 22093367-2 2012 This activity is compromised when vitamin B12 concentration is low because methionine synthase activity is reduced, lowering the concentration of S-adenosyl methionine (SAM) which in turn may diminish DNA methylation and cause folate to become unavailable for the conversion of dUMP to dTMP. S-Adenosylmethionine 169-172 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 75-94 16614482-3 2006 The evidence indicates that the critical site of B12 function in nerve tissue is in the enzyme, methionine synthase, in a system which requires S-adenosylmethionine. S-Adenosylmethionine 144-164 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 96-115 17477549-3 2007 On the basis of sequence similarity with Escherichia coli cobalamin-dependent MS (MetH), human MS comprises four discrete functional modules that bind from the N- to C-terminus, respectively, homocysteine, methyltetrahydrofolate, cobalamin, and S-adenosylmethionine (AdoMet). S-Adenosylmethionine 245-265 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 78-80 17477549-3 2007 On the basis of sequence similarity with Escherichia coli cobalamin-dependent MS (MetH), human MS comprises four discrete functional modules that bind from the N- to C-terminus, respectively, homocysteine, methyltetrahydrofolate, cobalamin, and S-adenosylmethionine (AdoMet). S-Adenosylmethionine 267-273 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 78-80 16614482-5 2006 Evidence is reviewed which suggests that there is an analogy between the two systems and that S-adenosyl methionine may catalyze a rearrangement of homocysteine on methionine synthase giving rise to iso- or beta-methionine. S-Adenosylmethionine 96-115 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 164-183 11406421-1 2001 Because polymorphisms in the methyl group metabolism genes methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and cystathione beta-synthetase (CBS) affect plasma homocysteine levels and intracellular concentrations of S-adenosylmethionine (SAM), they modify the susceptibility to cardiovascular diseases and cancer. S-Adenosylmethionine 239-259 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 105-124 11406421-1 2001 Because polymorphisms in the methyl group metabolism genes methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and cystathione beta-synthetase (CBS) affect plasma homocysteine levels and intracellular concentrations of S-adenosylmethionine (SAM), they modify the susceptibility to cardiovascular diseases and cancer. S-Adenosylmethionine 261-264 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 105-124 11295154-2 2001 This activity is compromised when Vitamin B12 (B12) concentration is low because methionine synthase activity is reduced, lowering the concentration of S-adenosyl methionine (SAM) which in turn may diminish DNA methylation and cause folate to become unavailable for the conversion of dUMP to dTMP. S-Adenosylmethionine 152-173 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 81-100 8939751-0 1996 The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12. S-Adenosylmethionine 76-94 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 42-61 11074524-2 2000 A possible cause underlying altered DNA methylation could be an insufficient level of S-adenosylmethionine as a consequence of nutritional imbalances or of weaker alleles of genes for its synthesis, i.e., encoding methylene-tetrahydrofolate reductase (MTHFR), methionine synthase (MS), and beta-cystathione synthetase (CBS). S-Adenosylmethionine 86-106 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 260-279 9201956-0 1997 Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine. S-Adenosylmethionine 148-166 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 0-39 8939751-7 1996 The structures of the AdoMet binding site and the cobalamin-binding domains (previously determined) provide a starting point for understanding the methyl transfer reactions of methionine synthase. S-Adenosylmethionine 22-28 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 176-195 30693532-4 2019 Methionine synthase catalyzes the methyl-Cbl dependent (re)methylation of homocysteine to methionine within the methionine cycle; a reaction required to produce this essential amino acid and generate S-adenosylmethionine, the most important cellular methyl-donor. S-Adenosylmethionine 200-220 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 0-19 8687414-1 1996 Vitamin B12-dependent methionine synthase is an important enzyme for sulphur amino acid, folate polyamine metabolism, S-adenosylmethionine metabolism and also in the methylation pathway of DNA, RNA, proteins and lipids. S-Adenosylmethionine 118-138 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 0-41 7961628-5 1994 This enzyme, like the methionine synthase from Escherichia coli is dependent on S-adenosylmethionine for activity. S-Adenosylmethionine 80-100 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 22-41 3076439-1 1988 S-Adenosylmethionine (SAM)-dependent activations of pyruvate formate-lyase, lysine 2,3-aminomutase and cobalamin-dependent methionine synthase are discussed. S-Adenosylmethionine 0-20 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 103-142 3076439-1 1988 S-Adenosylmethionine (SAM)-dependent activations of pyruvate formate-lyase, lysine 2,3-aminomutase and cobalamin-dependent methionine synthase are discussed. S-Adenosylmethionine 22-25 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 103-142 8904527-4 1996 Methionine synthase converts cellular homocysteine to methionine and is a major enzyme in the biosynthetic pathways for folates, S-adenosylmethionine and biological methylations, sulphur amino acids and polyamines. S-Adenosylmethionine 129-149 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 0-19 34592146-7 2021 Vitamin B12 has this protective effect by acting as a cofactor for methionine synthase, impacting the methionine/S-adenosylmethionine (SAMe) cycle. S-Adenosylmethionine 115-133 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 67-86 30676783-1 2019 Methionine synthase encoded by the MTR gene is one of the key enzymes involved in the SAM (S- Adenosyl Methionine) cycle catalyzing the conversion of homocysteine to methionine. S-Adenosylmethionine 92-113 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 0-19 29733595-0 2018 Water-Mediated Carbon-Oxygen Hydrogen Bonding Facilitates S-Adenosylmethionine Recognition in the Reactivation Domain of Cobalamin-Dependent Methionine Synthase. S-Adenosylmethionine 58-78 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 121-160 29562169-1 2018 Vitamin B12 functions as a cofactor for methionine synthase to produce the anabolic methyl donor S-adenosylmethionine (SAM) and for methylmalonyl-CoA mutase to catabolize the short-chain fatty acid propionate. S-Adenosylmethionine 97-117 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 40-59