PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7703232-7 1995 The distinctive difference between the enzyme forms was also the higher affinity of MB-COMT for the coenzyme S-adenosyl-L-methionine (AdoMet). S-Adenosylmethionine 109-132 catechol-O-methyltransferase Homo sapiens 87-91 7703232-7 1995 The distinctive difference between the enzyme forms was also the higher affinity of MB-COMT for the coenzyme S-adenosyl-L-methionine (AdoMet). S-Adenosylmethionine 134-140 catechol-O-methyltransferase Homo sapiens 87-91 7897657-1 1995 The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyl-transferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively. S-Adenosylmethionine 148-169 catechol-O-methyltransferase Homo sapiens 51-80 7897657-1 1995 The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyl-transferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively. S-Adenosylmethionine 148-169 catechol-O-methyltransferase Homo sapiens 82-86 7897657-1 1995 The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyl-transferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively. S-Adenosylmethionine 171-177 catechol-O-methyltransferase Homo sapiens 51-80 7897657-1 1995 The DNA methyltransferases, M.HhaI and M.TaqI, and catechol O-methyl-transferase (COMT) catalyze the transfer of a methyl group from the cofactor S-adenosyl-L-methionine (AdoMet) to carbon-5 of cytosine, to nitrogen-6 of adenine, and to a hydroxyl group of catechol, respectively. S-Adenosylmethionine 171-177 catechol-O-methyltransferase Homo sapiens 82-86 7773746-4 1995 Structural comparison of HhaI C5-cytosine methyltransferase, TaqI N6-adenine methyltransferase, and catechol O-methyltransferase reveals a common catalytic domain structure, which might be universal among S-adenosyl-L-methionine (SAM)-dependent methyltransferases. S-Adenosylmethionine 207-228 catechol-O-methyltransferase Homo sapiens 61-128 7773746-4 1995 Structural comparison of HhaI C5-cytosine methyltransferase, TaqI N6-adenine methyltransferase, and catechol O-methyltransferase reveals a common catalytic domain structure, which might be universal among S-adenosyl-L-methionine (SAM)-dependent methyltransferases. S-Adenosylmethionine 230-233 catechol-O-methyltransferase Homo sapiens 61-128 3753600-11 1986 Based on the above results, a catechol-binding site model for catechol O-methyltransferase is proposed in which the two phenolic hydroxyl groups of catechol substrates are postulated to be approximately equally spaced from the methyl group of the cosubstrate S-adenosylmethionine. S-Adenosylmethionine 259-279 catechol-O-methyltransferase Homo sapiens 62-90 1590912-5 1992 This hypothesis was tested by reacting SAM, MPP+, or MPTP with dopamine in the presence of catechol-O-methyltransferase and measuring the methylated product of dopamine produced. S-Adenosylmethionine 39-42 catechol-O-methyltransferase Homo sapiens 91-119 2128841-3 1990 However, the corresponding succinimide analogue shows a reversible inhibition of COMT, which is competitive with pyrocatecholphthalein and non-competitive with AdoMet. S-Adenosylmethionine 160-166 catechol-O-methyltransferase Homo sapiens 81-85 34679357-3 2021 The catechol O-methyltransferase (COMT) gene is located within the 22q11.2 region, and its product is an enzyme involved in transferring a methyl group from S-adenosylmethionine to catecholamines, including dopamine. S-Adenosylmethionine 157-177 catechol-O-methyltransferase Homo sapiens 4-32 34679357-3 2021 The catechol O-methyltransferase (COMT) gene is located within the 22q11.2 region, and its product is an enzyme involved in transferring a methyl group from S-adenosylmethionine to catecholamines, including dopamine. S-Adenosylmethionine 157-177 catechol-O-methyltransferase Homo sapiens 34-38 16668418-1 1991 S-Adenosyl-l-methionine:caffeic acid 3-O-methyltransferase (COMT, EC 2.1.1.6) catalyzes the conversion of caffeic acid to ferulic acid, a key step in the biosynthesis of lignin monomers. S-Adenosylmethionine 0-23 catechol-O-methyltransferase Homo sapiens 60-64 2736320-4 1989 Human erythrocyte soluble form of COMT had Km values of 6.1 microM and 26.0 microM for S-adenosyl-L-methionine and dihydroxybenzoic acid, respectively. S-Adenosylmethionine 87-110 catechol-O-methyltransferase Homo sapiens 34-38 7437264-7 1980 4 Kinetic studies with pooled uraemic plasma demonstrate that inhibition of COMT by uraemic plasma is uncompetitive with respect to both the catechol substrate and the methyl donor for the reaction, S-adenosyl-L-methionine. S-Adenosylmethionine 199-222 catechol-O-methyltransferase Homo sapiens 76-80 6491941-1 1984 Catechol derivatives, covalently joined to homocysteine by sulfide or sulfonium linkages, were synthesized as potential catechol O-methyltransferase multisubstrate inhibitors which might bridge the enzymatic binding sites for the catechol substrate and the amino acid portion of the methyl donor S-adenosylmethionine. S-Adenosylmethionine 296-316 catechol-O-methyltransferase Homo sapiens 120-148 6509362-1 1984 The formation of a stably linked complex of tritiated S-adenosyl-L-methionine (AdoMet) and catechol O-methyltransferase (COMT) has been achieved by irradiating the enzyme and ligand in Tris-HCl buffer (pH 7.5) with ultraviolet light at 254 nm. S-Adenosylmethionine 54-77 catechol-O-methyltransferase Homo sapiens 121-125 6509362-1 1984 The formation of a stably linked complex of tritiated S-adenosyl-L-methionine (AdoMet) and catechol O-methyltransferase (COMT) has been achieved by irradiating the enzyme and ligand in Tris-HCl buffer (pH 7.5) with ultraviolet light at 254 nm. S-Adenosylmethionine 79-85 catechol-O-methyltransferase Homo sapiens 121-125 6337144-5 1983 These results indicate that the incorporation is occurring at the S-adenosylmethionine binding site in the catechol O-methyltransferase. S-Adenosylmethionine 66-86 catechol-O-methyltransferase Homo sapiens 107-135 6272977-7 1981 When the Ames mutagenesis assay was supplemented with COMT/SAM, a 36% reduction was observed in the number of revertant colonies induced by the microsomal oxidation of BP. S-Adenosylmethionine 59-62 catechol-O-methyltransferase Homo sapiens 54-58 719895-0 1978 Influence of endogenous S-adenosylmethionine on the determination of catechol O-methyltransferase activity in red blood cells. S-Adenosylmethionine 24-44 catechol-O-methyltransferase Homo sapiens 69-97 455720-1 1979 A radiometric assay for catechol-O-methyltransferase (COMT) activity in human erythrocytes is described that employs 2-hydroxy[3H]estrone, and non-radiolabeled S-adenosylmethionine (SAM) as the cosubstrates. S-Adenosylmethionine 160-180 catechol-O-methyltransferase Homo sapiens 24-52 455720-1 1979 A radiometric assay for catechol-O-methyltransferase (COMT) activity in human erythrocytes is described that employs 2-hydroxy[3H]estrone, and non-radiolabeled S-adenosylmethionine (SAM) as the cosubstrates. S-Adenosylmethionine 160-180 catechol-O-methyltransferase Homo sapiens 54-58 455720-1 1979 A radiometric assay for catechol-O-methyltransferase (COMT) activity in human erythrocytes is described that employs 2-hydroxy[3H]estrone, and non-radiolabeled S-adenosylmethionine (SAM) as the cosubstrates. S-Adenosylmethionine 182-185 catechol-O-methyltransferase Homo sapiens 24-52 455720-1 1979 A radiometric assay for catechol-O-methyltransferase (COMT) activity in human erythrocytes is described that employs 2-hydroxy[3H]estrone, and non-radiolabeled S-adenosylmethionine (SAM) as the cosubstrates. S-Adenosylmethionine 182-185 catechol-O-methyltransferase Homo sapiens 54-58 487592-2 1979 Noradrenaline and adrenaline are converted to their O-methylated analogues, normethanephrine and metanephrine, by the enzyme catechol O-methyltransferase in the presence of tritiated S-adenosyl-L-methionine. S-Adenosylmethionine 183-206 catechol-O-methyltransferase Homo sapiens 125-153 978675-3 1976 Structural analogues of S-adenosyl-L-methionine (SAM), with modifications in the amino acid, sugar, or base portions of the molecule, have been synthesized and evaluated as either inhibitors and/or substrates for the enzymes catechol O-methyltransferase, phenylethanolamine N-methyltransferase, histamine N-methyltransferase, and hydroxyindole O-methyltransferase. S-Adenosylmethionine 24-47 catechol-O-methyltransferase Homo sapiens 225-253 978675-3 1976 Structural analogues of S-adenosyl-L-methionine (SAM), with modifications in the amino acid, sugar, or base portions of the molecule, have been synthesized and evaluated as either inhibitors and/or substrates for the enzymes catechol O-methyltransferase, phenylethanolamine N-methyltransferase, histamine N-methyltransferase, and hydroxyindole O-methyltransferase. S-Adenosylmethionine 49-52 catechol-O-methyltransferase Homo sapiens 225-253 32492152-1 2020 Human catechol-O-methyltransferase (COMT), a key enzyme related to neurotransmitter metabolism, catalyzes a methyl transfer from S-adenosylmethionine (SAM) to catechol. S-Adenosylmethionine 129-149 catechol-O-methyltransferase Homo sapiens 6-34 3250-1 1976 Catechol O-methyltransferase of lysed human red blood cells was assayed under optimal conditions, using saturating concentrations of the substrates, S-adenosyl-L-methionine and 3-4-dihydroxybenzoic acid. S-Adenosylmethionine 149-172 catechol-O-methyltransferase Homo sapiens 0-28 239677-6 1975 Human catechol O-methyltransferase exhibited lower Km values than did the rat enzyme for S-adenosyl-L-methionine, dopamine and dihydroxybenzoic acid. S-Adenosylmethionine 89-112 catechol-O-methyltransferase Homo sapiens 6-34 34027136-1 2021 Catechol O-methyltransferase, an enzyme involved in the metabolism of catechol containing compounds, catalyzes the transfer of a methyl group between S-adenosylmethionine and the hydroxyl groups of the catechol. S-Adenosylmethionine 150-170 catechol-O-methyltransferase Homo sapiens 0-28 32492152-1 2020 Human catechol-O-methyltransferase (COMT), a key enzyme related to neurotransmitter metabolism, catalyzes a methyl transfer from S-adenosylmethionine (SAM) to catechol. S-Adenosylmethionine 129-149 catechol-O-methyltransferase Homo sapiens 36-40 32492152-1 2020 Human catechol-O-methyltransferase (COMT), a key enzyme related to neurotransmitter metabolism, catalyzes a methyl transfer from S-adenosylmethionine (SAM) to catechol. S-Adenosylmethionine 151-154 catechol-O-methyltransferase Homo sapiens 6-34 32492152-1 2020 Human catechol-O-methyltransferase (COMT), a key enzyme related to neurotransmitter metabolism, catalyzes a methyl transfer from S-adenosylmethionine (SAM) to catechol. S-Adenosylmethionine 151-154 catechol-O-methyltransferase Homo sapiens 36-40 32371482-1 2020 Human catechol O-methyltransferase (COMT) has emerged as a model for understanding enzyme-catalyzed methyl transfer from S-adenosylmethionine (AdoMet) to small-molecule catecholate acceptors. S-Adenosylmethionine 121-141 catechol-O-methyltransferase Homo sapiens 6-34 32691671-6 2021 Initially, we analyzed the flexibility of COMT and defined its main conformations in solution regarding the absence (system I) and presence of the S-adenosyl-L-methionine (SAM) cofactor (system II) through molecular dynamics (MD) simulations. S-Adenosylmethionine 147-170 catechol-O-methyltransferase Homo sapiens 42-46 32691671-6 2021 Initially, we analyzed the flexibility of COMT and defined its main conformations in solution regarding the absence (system I) and presence of the S-adenosyl-L-methionine (SAM) cofactor (system II) through molecular dynamics (MD) simulations. S-Adenosylmethionine 172-175 catechol-O-methyltransferase Homo sapiens 42-46 32371482-1 2020 Human catechol O-methyltransferase (COMT) has emerged as a model for understanding enzyme-catalyzed methyl transfer from S-adenosylmethionine (AdoMet) to small-molecule catecholate acceptors. S-Adenosylmethionine 121-141 catechol-O-methyltransferase Homo sapiens 36-40 27939670-6 2017 The catfish Comt shared conserved putative structural regions important for S-adenosyl methionine (AdoMet)- and catechol-binding, transmembrane regions, two glycosylation sites (N-65 and N-91) at the N-terminus and two phosphorylation sites (Ser-235 and Thr-240) at the C-terminus. S-Adenosylmethionine 99-105 catechol-O-methyltransferase Homo sapiens 12-16 31869215-3 2020 HTS with a drug repositioning library revealed the importance of catechol-O-methyltransferase (COMT) and its substrates in controlling the SAM concentrations and histone methylation levels in colorectal tumor cells. S-Adenosylmethionine 139-142 catechol-O-methyltransferase Homo sapiens 65-93 31869215-3 2020 HTS with a drug repositioning library revealed the importance of catechol-O-methyltransferase (COMT) and its substrates in controlling the SAM concentrations and histone methylation levels in colorectal tumor cells. S-Adenosylmethionine 139-142 catechol-O-methyltransferase Homo sapiens 95-99 30935952-4 2019 Oleacein could be superimposed onto the catechol-binding site of COMT, maintaining the interactions with the atomic positions involved in methyl transfer from the S-adenosyl-L-methionine cofactor. S-Adenosylmethionine 163-186 catechol-O-methyltransferase Homo sapiens 65-69 31708229-8 2020 A detailed guide regarding inhibition of S-adenosyl-l-methionine, catalyzing the transfer of the methyl group by COMT is also represented. S-Adenosylmethionine 41-64 catechol-O-methyltransferase Homo sapiens 113-117 32378542-2 2020 All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor). S-Adenosylmethionine 130-150 catechol-O-methyltransferase Homo sapiens 24-28 32378542-2 2020 All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor). S-Adenosylmethionine 130-150 catechol-O-methyltransferase Homo sapiens 120-124 32378542-2 2020 All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor). S-Adenosylmethionine 130-150 catechol-O-methyltransferase Homo sapiens 120-124 32378542-2 2020 All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor). S-Adenosylmethionine 152-155 catechol-O-methyltransferase Homo sapiens 24-28 32378542-2 2020 All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor). S-Adenosylmethionine 152-155 catechol-O-methyltransferase Homo sapiens 120-124 32378542-2 2020 All clinically approved COMT inhibitors bring a 5-substituted-3-nitrocatechol ring as a pharmacophore, and they bind to COMT with S-adenosylmethionine (SAM) and an Mg2+ ion to form a quaternary complex (COMT/SAM/Mg2+/inhibitor). S-Adenosylmethionine 152-155 catechol-O-methyltransferase Homo sapiens 120-124 32378542-4 2020 Here, a new crystal structure of COMT complexed with nitecapone (5), SAM and Mg2+ is revealed. S-Adenosylmethionine 69-72 catechol-O-methyltransferase Homo sapiens 33-37 32378542-10 2020 This interaction seems to play a critical role in the affinity of the inhibitor and to stabilize the COMT/SAM/Mg2+/nitrocatechol inhibitor complex by fixing the flexible alpha2alpha3-loop. S-Adenosylmethionine 106-109 catechol-O-methyltransferase Homo sapiens 101-105 30157632-1 2018 Catechol- O-methyltransferase is an enzyme that catalyzes the methylation reaction of dopamine by S-adenosylmethionine, increasing the reaction rate by almost 16 orders of magnitude compared to the reaction in aqueous solution. S-Adenosylmethionine 98-118 catechol-O-methyltransferase Homo sapiens 0-29 28448141-0 2017 Correction to Design of Potent and Druglike Nonphenolic Inhibitors for Catechol O-Methyltransferase Derived from a Fragment Screening Approach Targeting the S-Adenosyl-l-methionine Pocket. S-Adenosylmethionine 157-180 catechol-O-methyltransferase Homo sapiens 71-99 27981425-0 2017 1H, 15N, 13C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-L-methionine and 3,5-dinitrocatechol. S-Adenosylmethionine 106-129 catechol-O-methyltransferase Homo sapiens 61-89 27981425-4 2017 Here we report the backbone 1H, 15N and 13C chemical shift assignments of S-COMT in complex with S-adenosyl-L-methionine, 3,5-dinitrocatechol and Mg2+. S-Adenosylmethionine 97-120 catechol-O-methyltransferase Homo sapiens 76-80 27826992-1 2017 Catechol-O-methyltransferase, COMT, is an important phase II enzyme catalyzing the transfer of a methyl-group from S-adenosylmethionine to a catechol-containing substrate molecule. S-Adenosylmethionine 115-135 catechol-O-methyltransferase Homo sapiens 0-28 27826992-1 2017 Catechol-O-methyltransferase, COMT, is an important phase II enzyme catalyzing the transfer of a methyl-group from S-adenosylmethionine to a catechol-containing substrate molecule. S-Adenosylmethionine 115-135 catechol-O-methyltransferase Homo sapiens 30-34 24450388-1 2013 Catechol-O-methyltransferase (COMT) is the enzyme which catalyzes the transfer of a methyl group from S-adenosylmethionine to catechols and catecholamines, like the neurotransmitters dopamine, epinephrine and norepinephrine. S-Adenosylmethionine 102-122 catechol-O-methyltransferase Homo sapiens 0-28 27685665-0 2016 Design of Potent and Druglike Nonphenolic Inhibitors for Catechol O-Methyltransferase Derived from a Fragment Screening Approach Targeting the S-Adenosyl-l-methionine Pocket. S-Adenosylmethionine 145-166 catechol-O-methyltransferase Homo sapiens 57-85 26253436-1 2015 Catechol-O-methyltransferase (COMT) is a methylation enzyme engaged in the degradation of dopamine and noradrenaline by catalyzing the transfer of a methyl group from S-adenosylmethionine. S-Adenosylmethionine 167-187 catechol-O-methyltransferase Homo sapiens 0-28 26253436-1 2015 Catechol-O-methyltransferase (COMT) is a methylation enzyme engaged in the degradation of dopamine and noradrenaline by catalyzing the transfer of a methyl group from S-adenosylmethionine. S-Adenosylmethionine 167-187 catechol-O-methyltransferase Homo sapiens 30-34 25388538-1 2015 The enzyme catechol O-methyltransferase (COMT) catalyzes the transfer of a methyl group from S-adenosylmethionine to dopamine and related catechols. S-Adenosylmethionine 93-113 catechol-O-methyltransferase Homo sapiens 11-39 25388538-1 2015 The enzyme catechol O-methyltransferase (COMT) catalyzes the transfer of a methyl group from S-adenosylmethionine to dopamine and related catechols. S-Adenosylmethionine 93-113 catechol-O-methyltransferase Homo sapiens 41-45 25159911-4 2015 The example analyzed here is the reaction catalyzed by catechol O-methyltransferase, a methyl transfer reaction from S-adenosylmethionine (SAM) to the nucleophilic oxygen atom of catecholate. S-Adenosylmethionine 117-137 catechol-O-methyltransferase Homo sapiens 55-83 25159911-4 2015 The example analyzed here is the reaction catalyzed by catechol O-methyltransferase, a methyl transfer reaction from S-adenosylmethionine (SAM) to the nucleophilic oxygen atom of catecholate. S-Adenosylmethionine 139-142 catechol-O-methyltransferase Homo sapiens 55-83 24847974-0 2014 A fragment-based approach to identifying S-adenosyl-l-methionine -competitive inhibitors of catechol O-methyl transferase (COMT). S-Adenosylmethionine 41-64 catechol-O-methyltransferase Homo sapiens 92-121 24847974-0 2014 A fragment-based approach to identifying S-adenosyl-l-methionine -competitive inhibitors of catechol O-methyl transferase (COMT). S-Adenosylmethionine 41-64 catechol-O-methyltransferase Homo sapiens 123-127 24450388-1 2013 Catechol-O-methyltransferase (COMT) is the enzyme which catalyzes the transfer of a methyl group from S-adenosylmethionine to catechols and catecholamines, like the neurotransmitters dopamine, epinephrine and norepinephrine. S-Adenosylmethionine 102-122 catechol-O-methyltransferase Homo sapiens 30-34 17880176-1 2007 Catechol-O-methyltransferase (COMT, EC 2.1.1.6) catalyzes the O-methylation of a wide array of catechol-containing substrates using s-adenosyl-L-methionine as the methyl donor. S-Adenosylmethionine 132-155 catechol-O-methyltransferase Homo sapiens 0-28 22349227-2 2012 Catechol-O-methyltransferase (COMT; EC 2.1.1.6) inactivates neurotransmitters by catalyzing the transfer of a methyl group from S-adenosylmethionine to catechols in the presence of Mg2+. S-Adenosylmethionine 128-148 catechol-O-methyltransferase Homo sapiens 0-28 23056605-1 2012 Catechol-O-methyltransferase (COMT) degrades catecholamines, such as dopamine and epinephrine, by methylating them in the presence of a divalent metal cation (usually Mg(II)), and S-adenosyl-L-methionine. S-Adenosylmethionine 180-203 catechol-O-methyltransferase Homo sapiens 0-28 23056605-1 2012 Catechol-O-methyltransferase (COMT) degrades catecholamines, such as dopamine and epinephrine, by methylating them in the presence of a divalent metal cation (usually Mg(II)), and S-adenosyl-L-methionine. S-Adenosylmethionine 180-203 catechol-O-methyltransferase Homo sapiens 30-34 21958159-1 2011 Human catechol-O-methyltransferase (COMT) catalyzes a methyl transfer from S-adenosylmethionine (AdoMet) to dopamine. S-Adenosylmethionine 75-95 catechol-O-methyltransferase Homo sapiens 6-34 21958159-1 2011 Human catechol-O-methyltransferase (COMT) catalyzes a methyl transfer from S-adenosylmethionine (AdoMet) to dopamine. S-Adenosylmethionine 75-95 catechol-O-methyltransferase Homo sapiens 36-40 21958159-1 2011 Human catechol-O-methyltransferase (COMT) catalyzes a methyl transfer from S-adenosylmethionine (AdoMet) to dopamine. S-Adenosylmethionine 97-103 catechol-O-methyltransferase Homo sapiens 6-34 21958159-1 2011 Human catechol-O-methyltransferase (COMT) catalyzes a methyl transfer from S-adenosylmethionine (AdoMet) to dopamine. S-Adenosylmethionine 97-103 catechol-O-methyltransferase Homo sapiens 36-40 21538606-2 2011 COMT catalyzes the transfer of an activated methyl group from S-adenosylmethionine (SAM) to its catechol substrates, such as L-dopa, in the presence of magnesium ions. S-Adenosylmethionine 62-82 catechol-O-methyltransferase Homo sapiens 0-4 21538606-2 2011 COMT catalyzes the transfer of an activated methyl group from S-adenosylmethionine (SAM) to its catechol substrates, such as L-dopa, in the presence of magnesium ions. S-Adenosylmethionine 84-87 catechol-O-methyltransferase Homo sapiens 0-4 21538606-3 2011 The molecular recognition properties of the SAM-binding site of COMT have been investigated only sparsely. S-Adenosylmethionine 44-47 catechol-O-methyltransferase Homo sapiens 64-68 21154325-1 2010 The enzyme catechol-O-methyltransferase (COMT) transfers a methyl group from S-adenosylmethionine to the benzene ring of catecholamines including the neurotransmitters dopamine, epinephrine and norepinephrine. S-Adenosylmethionine 77-97 catechol-O-methyltransferase Homo sapiens 11-39 21154325-1 2010 The enzyme catechol-O-methyltransferase (COMT) transfers a methyl group from S-adenosylmethionine to the benzene ring of catecholamines including the neurotransmitters dopamine, epinephrine and norepinephrine. S-Adenosylmethionine 77-97 catechol-O-methyltransferase Homo sapiens 41-45 18486144-6 2008 Here we describe the crystal structures of the 108V and 108M variants of the soluble form of human COMT bound with S-adenosylmethionine (SAM) and a substrate analog, 3,5-dinitrocatechol. S-Adenosylmethionine 115-135 catechol-O-methyltransferase Homo sapiens 99-103 18486144-6 2008 Here we describe the crystal structures of the 108V and 108M variants of the soluble form of human COMT bound with S-adenosylmethionine (SAM) and a substrate analog, 3,5-dinitrocatechol. S-Adenosylmethionine 137-140 catechol-O-methyltransferase Homo sapiens 99-103 17724020-7 2007 Inhibition of catechol-O-methyltransferase activity with tyrphostin AG1288 prevents both base-volatile product formation and protein labeling from methyl-labeled S-adenosylmethionine in heart, kidney, and liver, but not in testes or brain extracts. S-Adenosylmethionine 162-182 catechol-O-methyltransferase Homo sapiens 14-42 21304959-6 2011 COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor. S-Adenosylmethionine 118-138 catechol-O-methyltransferase Homo sapiens 0-4 21304959-6 2011 COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor. S-Adenosylmethionine 118-138 catechol-O-methyltransferase Homo sapiens 148-152 21304959-6 2011 COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor. S-Adenosylmethionine 140-143 catechol-O-methyltransferase Homo sapiens 0-4 21304959-6 2011 COMT has been shown to interact with methylenetetrahydrofolate reductase (MTHFR), which modulates the availability of S-adenosylmethionine (SAM), a COMT cofactor. S-Adenosylmethionine 140-143 catechol-O-methyltransferase Homo sapiens 148-152 21904625-0 2011 Structural mechanism of S-adenosyl methionine binding to catechol O-methyltransferase. S-Adenosylmethionine 24-45 catechol-O-methyltransferase Homo sapiens 57-85 18824331-4 2009 We have therefore investigated the efficacy of SAM-e in managing schizophrenia symptomatology in patients with the low activity COMT polymorphism. S-Adenosylmethionine 47-52 catechol-O-methyltransferase Homo sapiens 128-132 19077667-1 2009 Human catechol-O-methyltransferase (COMT; EC 2.1.1.6) catalyzes the transfer of the methyl group to a variety of endogenous and exogenous catechol substrates using S-adenosyl-L-methionine as the methyl donor. S-Adenosylmethionine 164-187 catechol-O-methyltransferase Homo sapiens 6-34 19077667-1 2009 Human catechol-O-methyltransferase (COMT; EC 2.1.1.6) catalyzes the transfer of the methyl group to a variety of endogenous and exogenous catechol substrates using S-adenosyl-L-methionine as the methyl donor. S-Adenosylmethionine 164-187 catechol-O-methyltransferase Homo sapiens 36-40 19020775-1 2008 Human catechol-O-methyltransferase (COMT, EC 2.1.1.6) catalyzes the transfer of the methyl group to a variety of endogenous and exogenous catechol substrates using S-adenosyl-L-methionine as the methyl donor. S-Adenosylmethionine 164-187 catechol-O-methyltransferase Homo sapiens 6-34 19020775-1 2008 Human catechol-O-methyltransferase (COMT, EC 2.1.1.6) catalyzes the transfer of the methyl group to a variety of endogenous and exogenous catechol substrates using S-adenosyl-L-methionine as the methyl donor. S-Adenosylmethionine 164-187 catechol-O-methyltransferase Homo sapiens 36-40 19020775-5 2008 Kinetic analysis showed that these new COMT variants had essentially the same kinetic characteristics and catalytic activity as the wild-type COMTs for the O-methylation of 2-hydroxyestradiol and 4-hydroxyestradiol in vitro, but they have asignificantly reduced thermostability at 37 degrees C. In addition, the mutant enzymes have different binding affinities for S-adenosyl-L-methionine compared with the wild-type COMTs. S-Adenosylmethionine 365-388 catechol-O-methyltransferase Homo sapiens 39-43 18474266-4 2008 COMT contains two tryptophan residues, W143 and W38Y, which are located in loops that border the S-adenosylmethionine (SAM) and catechol binding sites. S-Adenosylmethionine 97-117 catechol-O-methyltransferase Homo sapiens 0-4 18474266-4 2008 COMT contains two tryptophan residues, W143 and W38Y, which are located in loops that border the S-adenosylmethionine (SAM) and catechol binding sites. S-Adenosylmethionine 119-122 catechol-O-methyltransferase Homo sapiens 0-4 18064318-2 2007 Catechol-O-methyltransferase (COMT) is involved in the S-adenosylmethionine-dependent methylation of catecholamines and catecholestrogens and in this way contributes to homocysteine synthesis. S-Adenosylmethionine 57-75 catechol-O-methyltransferase Homo sapiens 0-28 18064318-2 2007 Catechol-O-methyltransferase (COMT) is involved in the S-adenosylmethionine-dependent methylation of catecholamines and catecholestrogens and in this way contributes to homocysteine synthesis. S-Adenosylmethionine 57-75 catechol-O-methyltransferase Homo sapiens 30-34 17907785-12 2007 Inclusion of the catechol-O-methyltransferase cofactor S-adenosylmethionine (SAM) in S-9 incubations also dramatically reduced the covalent binding of [(3)H]paroxetine, a finding that was consistent with O-methylation of the paroxetine-catechol metabolite to the corresponding guaiacol regioisomers in S-9 incubations. S-Adenosylmethionine 55-75 catechol-O-methyltransferase Homo sapiens 17-45 17907785-12 2007 Inclusion of the catechol-O-methyltransferase cofactor S-adenosylmethionine (SAM) in S-9 incubations also dramatically reduced the covalent binding of [(3)H]paroxetine, a finding that was consistent with O-methylation of the paroxetine-catechol metabolite to the corresponding guaiacol regioisomers in S-9 incubations. S-Adenosylmethionine 77-80 catechol-O-methyltransferase Homo sapiens 17-45 17880176-1 2007 Catechol-O-methyltransferase (COMT, EC 2.1.1.6) catalyzes the O-methylation of a wide array of catechol-containing substrates using s-adenosyl-L-methionine as the methyl donor. S-Adenosylmethionine 132-155 catechol-O-methyltransferase Homo sapiens 30-34 16475806-2 2006 While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia. S-Adenosylmethionine 142-162 catechol-O-methyltransferase Homo sapiens 61-65 16618795-6 2006 The major structural and chemical factors that determine the enzyme regioselectivity of O-methylation were identified, and the X-ray structure of the complex of COMT with S-adenosyl-l-methionine and BIA 8-176 is herein disclosed. S-Adenosylmethionine 171-194 catechol-O-methyltransferase Homo sapiens 161-165 16475806-2 2006 While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia. S-Adenosylmethionine 142-162 catechol-O-methyltransferase Homo sapiens 104-108 16475806-2 2006 While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia. S-Adenosylmethionine 142-162 catechol-O-methyltransferase Homo sapiens 104-108 16475806-2 2006 While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia. S-Adenosylmethionine 164-167 catechol-O-methyltransferase Homo sapiens 61-65 16475806-2 2006 While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia. S-Adenosylmethionine 164-167 catechol-O-methyltransferase Homo sapiens 104-108 16475806-2 2006 While the two proteins have similar kinetic properties, 108M COMT loses activity more rapidly than 108V COMT at 37 degrees C. The cosubstrate S-adenosylmethionine (SAM) stabilizes the activity of 108M COMT at 40 degrees C. The 108M allele has been associated with increased risk for breast cancer, obsessive-compulsive disorder, and aggressive and highly antisocial manifestations of schizophrenia. S-Adenosylmethionine 164-167 catechol-O-methyltransferase Homo sapiens 104-108 15124004-1 2004 The enzyme catechol-o-methyltransferase (COMT) transfers a methyl group from adenosylmethionine to catecholamines including the neurotransmitters dopamine, epinephrine and norepinephrine. S-Adenosylmethionine 77-95 catechol-O-methyltransferase Homo sapiens 11-39 16340382-1 2005 Metabolism of levodopa via the enzyme catechol-O-methyltransferase requires S-adenosylmethionine (SAM) as a methyl donor. S-Adenosylmethionine 76-96 catechol-O-methyltransferase Homo sapiens 38-66 16340382-1 2005 Metabolism of levodopa via the enzyme catechol-O-methyltransferase requires S-adenosylmethionine (SAM) as a methyl donor. S-Adenosylmethionine 98-101 catechol-O-methyltransferase Homo sapiens 38-66 15614425-2 2005 Levodopa is metabolised via O-methylation by catechol-O-methyltransferase (COMT) using S-adenosyl-L-methionine (SAM) as the methyl donor, this leading to the subsequent formation of homocysteine. S-Adenosylmethionine 87-110 catechol-O-methyltransferase Homo sapiens 45-73 15614425-2 2005 Levodopa is metabolised via O-methylation by catechol-O-methyltransferase (COMT) using S-adenosyl-L-methionine (SAM) as the methyl donor, this leading to the subsequent formation of homocysteine. S-Adenosylmethionine 87-110 catechol-O-methyltransferase Homo sapiens 75-79 15614425-2 2005 Levodopa is metabolised via O-methylation by catechol-O-methyltransferase (COMT) using S-adenosyl-L-methionine (SAM) as the methyl donor, this leading to the subsequent formation of homocysteine. S-Adenosylmethionine 112-115 catechol-O-methyltransferase Homo sapiens 45-73 15614425-2 2005 Levodopa is metabolised via O-methylation by catechol-O-methyltransferase (COMT) using S-adenosyl-L-methionine (SAM) as the methyl donor, this leading to the subsequent formation of homocysteine. S-Adenosylmethionine 112-115 catechol-O-methyltransferase Homo sapiens 75-79 16045352-4 2005 In this article we are reporting static and dynamic aspects of the enzyme catalysis in a bimolecular reaction, namely a methyl transfer from S-adenosylmethionine to the hydroxylate oxygen of a substituted catechol catalyzed by catechol O-methyltransferase. S-Adenosylmethionine 141-161 catechol-O-methyltransferase Homo sapiens 227-255 15124004-1 2004 The enzyme catechol-o-methyltransferase (COMT) transfers a methyl group from adenosylmethionine to catecholamines including the neurotransmitters dopamine, epinephrine and norepinephrine. S-Adenosylmethionine 77-95 catechol-O-methyltransferase Homo sapiens 41-45 12533089-3 2003 However, patients with Parkinson disease (PD) may have elevated homocysteine levels resulting from methylation of levodopa and dopamine by catechol O-methyltransferase, an enzyme that uses S-adenosylmethionine as a methyl donor and yields S-adenosylhomocysteine. S-Adenosylmethionine 189-209 catechol-O-methyltransferase Homo sapiens 139-167 12842102-2 2003 In this method, the methyl group of S-adenosyl-L-methionine was enzymatically transferred to esculetin with the aid of catechol-O-methyltransferase and then the resulting scopoletin was extracted with n-hexane:ethyl acetate (7:3, v/v) and measured by high-performance liquid chromatography with Si 60 column and fluorometric detection with excitation and emission wavelengths at 347 and 415 nm, respectively. S-Adenosylmethionine 36-59 catechol-O-methyltransferase Homo sapiens 119-147 9681662-3 1998 RESULTS: The activity of COMT was measured with 3,4-dihydroxybenzoic acid (242 micromol x l(-1)), the methyl acceptor substrate, and adenosyl-L-methionine (44 micromol x l(-1)), the methyl donor substrate. S-Adenosylmethionine 133-154 catechol-O-methyltransferase Homo sapiens 25-29 12450669-1 2002 Catechol O-methyltransferase (COMT) transfers a methyl group from S-adenosyl-L-methionine to the catechol substrate in the presence of magnesium. S-Adenosylmethionine 66-89 catechol-O-methyltransferase Homo sapiens 0-28 12450669-1 2002 Catechol O-methyltransferase (COMT) transfers a methyl group from S-adenosyl-L-methionine to the catechol substrate in the presence of magnesium. S-Adenosylmethionine 66-89 catechol-O-methyltransferase Homo sapiens 30-34 11577006-1 2001 Catechol-O-methyltransferase (COMT) catalyzes the O-methylation of catechol estrogens (CEs), using S-adenosylmethionine (SAM) as a methyl donor. S-Adenosylmethionine 99-119 catechol-O-methyltransferase Homo sapiens 0-28 11577006-1 2001 Catechol-O-methyltransferase (COMT) catalyzes the O-methylation of catechol estrogens (CEs), using S-adenosylmethionine (SAM) as a methyl donor. S-Adenosylmethionine 99-119 catechol-O-methyltransferase Homo sapiens 30-34 11577006-1 2001 Catechol-O-methyltransferase (COMT) catalyzes the O-methylation of catechol estrogens (CEs), using S-adenosylmethionine (SAM) as a methyl donor. S-Adenosylmethionine 121-124 catechol-O-methyltransferase Homo sapiens 0-28 11577006-1 2001 Catechol-O-methyltransferase (COMT) catalyzes the O-methylation of catechol estrogens (CEs), using S-adenosylmethionine (SAM) as a methyl donor. S-Adenosylmethionine 121-124 catechol-O-methyltransferase Homo sapiens 30-34 11577006-3 2001 Folate, whose intake levels have also been associated with breast cancer risk, and other micronutrients in the folate metabolic pathway influence levels of SAM and S-adenosylhomocysteine (SAH), a COMT inhibitor generated by the demethylation of SAM. S-Adenosylmethionine 156-159 catechol-O-methyltransferase Homo sapiens 196-200 10950844-3 2000 When (-)-epicatechin was used as substrate, its O-methylation by human placental COMT showed dependence on incubation time, cytosolic protein concentration, incubation pH, and concentration of S-adenosyl-L-methionine (the methyl donor). S-Adenosylmethionine 193-216 catechol-O-methyltransferase Homo sapiens 81-85 10950844-5 2000 Additional analysis revealed that COMT-catalyzed O-methylation of (-)-epicatechin and (-)-epigallocatechin was strongly inhibited in a concentration-dependent manner by S-adenosyl-L-homocysteine (IC(50) = 3.2-5.7 microM), a demethylated product of S-adenosyl-L-methionine. S-Adenosylmethionine 248-271 catechol-O-methyltransferase Homo sapiens 34-38 10692500-8 2000 Furthermore, the primary metabolite of L-dopa formed by COMT, 3-O-methyldopa, and the methyl group donor S-adenosyl-L-methionine used by COMT did not alter THir neuron survival and L-dopa-induced toxicity, respectively, with concentrations up to 100 microM. S-Adenosylmethionine 107-128 catechol-O-methyltransferase Homo sapiens 137-141 12075857-2 2002 Since COMT requires Mg2+ and S-adenosylmethionine as methyl donor for this transmethylating process, COMT converts S-adenosylmethionine to S-adenosylhomocysteine and subsequent homocysteine. S-Adenosylmethionine 29-49 catechol-O-methyltransferase Homo sapiens 6-10 12075857-2 2002 Since COMT requires Mg2+ and S-adenosylmethionine as methyl donor for this transmethylating process, COMT converts S-adenosylmethionine to S-adenosylhomocysteine and subsequent homocysteine. S-Adenosylmethionine 29-49 catechol-O-methyltransferase Homo sapiens 101-105 12075857-2 2002 Since COMT requires Mg2+ and S-adenosylmethionine as methyl donor for this transmethylating process, COMT converts S-adenosylmethionine to S-adenosylhomocysteine and subsequent homocysteine. S-Adenosylmethionine 115-135 catechol-O-methyltransferase Homo sapiens 6-10 12075857-2 2002 Since COMT requires Mg2+ and S-adenosylmethionine as methyl donor for this transmethylating process, COMT converts S-adenosylmethionine to S-adenosylhomocysteine and subsequent homocysteine. S-Adenosylmethionine 115-135 catechol-O-methyltransferase Homo sapiens 101-105 11223018-0 2001 COMT-dependent protection of dopaminergic neurons by methionine, dimethionine and S-adenosylmethionine (SAM) against L-dopa toxicity in vitro. S-Adenosylmethionine 82-102 catechol-O-methyltransferase Homo sapiens 0-4 10064789-2 1999 COMT activity was evaluated by the ability to methylate adrenaline (0.1 to 2000 microM) to metanephrine in the presence of a saturating concentration of the methyl donor (S-adenosyl-l-methionine). S-Adenosylmethionine 171-194 catechol-O-methyltransferase Homo sapiens 0-4