PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3223955-3 1988 The only known mammalian pathway for the synthesis de novo of choline molecules is catalysed by phosphatidylethanolamine N-methyltransferase (PeMT), which synthesizes phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor. S-Adenosylmethionine 266-286 phosphatidylethanolamine N-methyltransferase Homo sapiens 96-140 23446897-1 2013 BACKGROUND: Phosphatidylcholine (PC) produced via the S-adenosylmethionine-dependent phosphatidylethanolamine (PE) N-methyltransferase (PEMT) pathway is enriched with docosahexaenoic acid (DHA). S-Adenosylmethionine 56-74 phosphatidylethanolamine N-methyltransferase Homo sapiens 136-140 21068006-6 2011 Finally, we present a multiple isotopomer distribution analysis approach, based on transfer of deuterated methyl groups to S-adenosylmethionine and subsequent sequential methylations of PE, to quantify absolute flux rates through the PEMT pathway that are applicable to studies of liver dysfunction in clinical studies. S-Adenosylmethionine 123-143 phosphatidylethanolamine N-methyltransferase Homo sapiens 234-238 12431977-2 2003 Phosphatidylethanolamine N-methyltransferase (PEMT) catalyzes each transmethylation reaction, and S-adenosylmethionine is the methyl group donor. S-Adenosylmethionine 98-118 phosphatidylethanolamine N-methyltransferase Homo sapiens 0-44 12431977-2 2003 Phosphatidylethanolamine N-methyltransferase (PEMT) catalyzes each transmethylation reaction, and S-adenosylmethionine is the methyl group donor. S-Adenosylmethionine 98-118 phosphatidylethanolamine N-methyltransferase Homo sapiens 46-50 7943660-4 1994 Phosphatidylethanolamine N-methyltransferase activity was measured in sequential percutaneous needle liver biopsies by the conversion of phosphatidylethanolamine to phosphatidylcholine, using radioactive S-adenosylmethionine as a methyl donor. S-Adenosylmethionine 204-224 phosphatidylethanolamine N-methyltransferase Homo sapiens 0-44 15695433-1 2005 The betaine biosynthesis pathway of betaine-accumulating plants involves choline monooxygenase (CMO) as the key enzyme and phosphoethanolamine N-methyltransferase (PEAMT), which require S-adenosyl-L-methionine (SAM) as a methyl donor. S-Adenosylmethionine 186-209 phosphatidylethanolamine N-methyltransferase Homo sapiens 123-162 15695433-1 2005 The betaine biosynthesis pathway of betaine-accumulating plants involves choline monooxygenase (CMO) as the key enzyme and phosphoethanolamine N-methyltransferase (PEAMT), which require S-adenosyl-L-methionine (SAM) as a methyl donor. S-Adenosylmethionine 186-209 phosphatidylethanolamine N-methyltransferase Homo sapiens 164-169 15695433-1 2005 The betaine biosynthesis pathway of betaine-accumulating plants involves choline monooxygenase (CMO) as the key enzyme and phosphoethanolamine N-methyltransferase (PEAMT), which require S-adenosyl-L-methionine (SAM) as a methyl donor. S-Adenosylmethionine 211-214 phosphatidylethanolamine N-methyltransferase Homo sapiens 164-169 12842883-0 2003 Molecular dissection of the S-adenosylmethionine-binding site of phosphatidylethanolamine N-methyltransferase. S-Adenosylmethionine 28-48 phosphatidylethanolamine N-methyltransferase Homo sapiens 65-109 12842883-4 2003 To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet). S-Adenosylmethionine 205-225 phosphatidylethanolamine N-methyltransferase Homo sapiens 25-29 12842883-4 2003 To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet). S-Adenosylmethionine 205-225 phosphatidylethanolamine N-methyltransferase Homo sapiens 83-87 12842883-4 2003 To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet). S-Adenosylmethionine 227-233 phosphatidylethanolamine N-methyltransferase Homo sapiens 25-29 12842883-4 2003 To gain insight into the PEMT transmethylation reaction and the mechanism by which PEMT regulates homocysteine levels, we sought to define residues that are required for binding of the methyl group donor, S-adenosylmethionine (AdoMet). S-Adenosylmethionine 227-233 phosphatidylethanolamine N-methyltransferase Homo sapiens 83-87 3223955-3 1988 The only known mammalian pathway for the synthesis de novo of choline molecules is catalysed by phosphatidylethanolamine N-methyltransferase (PeMT), which synthesizes phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor. S-Adenosylmethionine 266-286 phosphatidylethanolamine N-methyltransferase Homo sapiens 142-146 3223955-3 1988 The only known mammalian pathway for the synthesis de novo of choline molecules is catalysed by phosphatidylethanolamine N-methyltransferase (PeMT), which synthesizes phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor. S-Adenosylmethionine 288-294 phosphatidylethanolamine N-methyltransferase Homo sapiens 96-140 3223955-3 1988 The only known mammalian pathway for the synthesis de novo of choline molecules is catalysed by phosphatidylethanolamine N-methyltransferase (PeMT), which synthesizes phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor. S-Adenosylmethionine 288-294 phosphatidylethanolamine N-methyltransferase Homo sapiens 142-146 3025802-1 1986 Human lymphocyte and granulocyte membranes contain an enzyme, phosphatidylethanolamine N-methyltransferase (PEMT), which catalyzes the transfer of a methyl group from S-adenosylmethionine to the polar head group of phosphatidylethanolamine to form phosphatidylmonomethylethanolamine. S-Adenosylmethionine 167-187 phosphatidylethanolamine N-methyltransferase Homo sapiens 62-106 3025802-1 1986 Human lymphocyte and granulocyte membranes contain an enzyme, phosphatidylethanolamine N-methyltransferase (PEMT), which catalyzes the transfer of a methyl group from S-adenosylmethionine to the polar head group of phosphatidylethanolamine to form phosphatidylmonomethylethanolamine. S-Adenosylmethionine 167-187 phosphatidylethanolamine N-methyltransferase Homo sapiens 108-112 3025802-3 1986 Granulocyte membrane PEMT has Km for S-adenosylmethionine of 4.4 microM and specific activity 0.54 +/- 0.51 pmol/mg protein/15 min, is inhibited by S-adenosylhomocysteine, displays optimal activity at pH 8.0-9.5, and is stimulated by isoproterenol greater than epinephrine greater than norepinephrine, but not by prostaglandin E1, serum-treated zymosan, formyl-methionyl-leucyl-phenylalanine, or adenosine 3":5" cyclic monophosphate. S-Adenosylmethionine 37-57 phosphatidylethanolamine N-methyltransferase Homo sapiens 21-25 32912785-5 2020 PEMT converts PE into PC using methyl group by S-adenosylmethionine (SAM) thus converted in S-adenosylhomocysteine (SAH). S-Adenosylmethionine 47-67 phosphatidylethanolamine N-methyltransferase Homo sapiens 0-4 6680524-1 1983 The catalysis by phosphatidylethanolamine methyltransferase (PEMT) of phosphatidylcholine (PC) synthesis by the successive methylation of phosphatidylethanolamine in the presence of S-adenosylmethionine (AdoMet) as methyl donor, was detected in actively myelinating mouse brains. S-Adenosylmethionine 182-202 phosphatidylethanolamine N-methyltransferase Homo sapiens 17-59 6680524-1 1983 The catalysis by phosphatidylethanolamine methyltransferase (PEMT) of phosphatidylcholine (PC) synthesis by the successive methylation of phosphatidylethanolamine in the presence of S-adenosylmethionine (AdoMet) as methyl donor, was detected in actively myelinating mouse brains. S-Adenosylmethionine 182-202 phosphatidylethanolamine N-methyltransferase Homo sapiens 61-65 6680524-1 1983 The catalysis by phosphatidylethanolamine methyltransferase (PEMT) of phosphatidylcholine (PC) synthesis by the successive methylation of phosphatidylethanolamine in the presence of S-adenosylmethionine (AdoMet) as methyl donor, was detected in actively myelinating mouse brains. S-Adenosylmethionine 204-210 phosphatidylethanolamine N-methyltransferase Homo sapiens 17-59 6680524-1 1983 The catalysis by phosphatidylethanolamine methyltransferase (PEMT) of phosphatidylcholine (PC) synthesis by the successive methylation of phosphatidylethanolamine in the presence of S-adenosylmethionine (AdoMet) as methyl donor, was detected in actively myelinating mouse brains. S-Adenosylmethionine 204-210 phosphatidylethanolamine N-methyltransferase Homo sapiens 61-65 4091805-1 1985 The activity of phosphatidylethanolamine N-methyltransferase (PeMT), an enzymic system that catalyses the synthesis of phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor, was examined in brain homogenates from rats of various ages. S-Adenosylmethionine 218-238 phosphatidylethanolamine N-methyltransferase Homo sapiens 16-60 4091805-1 1985 The activity of phosphatidylethanolamine N-methyltransferase (PeMT), an enzymic system that catalyses the synthesis of phosphatidylcholine (PtdCho) via sequential methylation of phosphatidylethanolamine (PtdEtn) using S-adenosylmethionine (AdoMet) as a methyl donor, was examined in brain homogenates from rats of various ages. S-Adenosylmethionine 240-246 phosphatidylethanolamine N-methyltransferase Homo sapiens 16-60 7219528-3 1981 Recently we and others have demonstrated that various preparations of mammalian brain contain enzymes, the phosphatidylethanolamine N-methyltransferase (PeMT), which catalyse the synthesis of phosphatidylcholine (PC), using S-adenosylmethionine (SAM) as a methyl donor for the stepwise methylation of phosphatidylethanolamine (PE). S-Adenosylmethionine 224-244 phosphatidylethanolamine N-methyltransferase Homo sapiens 107-151 7219528-3 1981 Recently we and others have demonstrated that various preparations of mammalian brain contain enzymes, the phosphatidylethanolamine N-methyltransferase (PeMT), which catalyse the synthesis of phosphatidylcholine (PC), using S-adenosylmethionine (SAM) as a methyl donor for the stepwise methylation of phosphatidylethanolamine (PE). S-Adenosylmethionine 224-244 phosphatidylethanolamine N-methyltransferase Homo sapiens 153-157 7219528-3 1981 Recently we and others have demonstrated that various preparations of mammalian brain contain enzymes, the phosphatidylethanolamine N-methyltransferase (PeMT), which catalyse the synthesis of phosphatidylcholine (PC), using S-adenosylmethionine (SAM) as a methyl donor for the stepwise methylation of phosphatidylethanolamine (PE). S-Adenosylmethionine 246-249 phosphatidylethanolamine N-methyltransferase Homo sapiens 107-151 7219528-3 1981 Recently we and others have demonstrated that various preparations of mammalian brain contain enzymes, the phosphatidylethanolamine N-methyltransferase (PeMT), which catalyse the synthesis of phosphatidylcholine (PC), using S-adenosylmethionine (SAM) as a methyl donor for the stepwise methylation of phosphatidylethanolamine (PE). S-Adenosylmethionine 246-249 phosphatidylethanolamine N-methyltransferase Homo sapiens 153-157 32912785-5 2020 PEMT converts PE into PC using methyl group by S-adenosylmethionine (SAM) thus converted in S-adenosylhomocysteine (SAH). S-Adenosylmethionine 69-72 phosphatidylethanolamine N-methyltransferase Homo sapiens 0-4