PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21036620-2 2010 To obtain novel inhibitors as tools for investigating the physiological function of members of the HMT family, we designed and synthesized novel inhibitors, which are amine analogues of adenosylmethionine (AdoMet; the cofactor utilized in the methylation reaction) bearing various alkylamino groups coupled via an ethylene linker. S-Adenosylmethionine 186-204 histamine N-methyltransferase Homo sapiens 99-102 26206890-2 2015 The enzyme histamine N-methyltransferase (HNMT) inactivates HA by transferring a methyl group from S-adenosyl-l-methionine to HA, and is the only well-known pathway for termination of neurotransmission actions of HA in mammalian central nervous system. S-Adenosylmethionine 99-122 histamine N-methyltransferase Homo sapiens 11-40 26206890-2 2015 The enzyme histamine N-methyltransferase (HNMT) inactivates HA by transferring a methyl group from S-adenosyl-l-methionine to HA, and is the only well-known pathway for termination of neurotransmission actions of HA in mammalian central nervous system. S-Adenosylmethionine 99-122 histamine N-methyltransferase Homo sapiens 42-46 21036620-2 2010 To obtain novel inhibitors as tools for investigating the physiological function of members of the HMT family, we designed and synthesized novel inhibitors, which are amine analogues of adenosylmethionine (AdoMet; the cofactor utilized in the methylation reaction) bearing various alkylamino groups coupled via an ethylene linker. S-Adenosylmethionine 206-212 histamine N-methyltransferase Homo sapiens 99-102 8147263-12 1993 When the concentration of the cosubstrate for the reaction, S-adenosyl-L-methionine, was varied in the presence of variable concentrations of pargyline, inhibition of HNMT by pargyline was noncompetitive with regard to the methyl donor, with Kii and Kis values of 1.23 and 0.95 mM, respectively. S-Adenosylmethionine 60-83 histamine N-methyltransferase Homo sapiens 167-171 18208517-1 2008 In the S-methylmethionine cycle of plants, homocysteine methyltransferase (HMT) catalyzes the formation of two molecules of methionine from homocysteine and S-methylmethionine, and methionine methyltransferase (MMT) catalyzes the formation of methionine from S-methylmethionine using S-adenosylmethionine as a methyl group donor. S-Adenosylmethionine 284-304 histamine N-methyltransferase Homo sapiens 43-73 18208517-1 2008 In the S-methylmethionine cycle of plants, homocysteine methyltransferase (HMT) catalyzes the formation of two molecules of methionine from homocysteine and S-methylmethionine, and methionine methyltransferase (MMT) catalyzes the formation of methionine from S-methylmethionine using S-adenosylmethionine as a methyl group donor. S-Adenosylmethionine 284-304 histamine N-methyltransferase Homo sapiens 75-78 11566133-8 2001 CONCLUSIONS: HNMT has a 2 domain structure including a consensus AdoMet binding domain, where the residue 105 is located on the surface, consistent with the kinetic data that the polymorphism does not affect overall protein stability at physiological temperatures but lowers K(M) values for AdoMet and histamine. S-Adenosylmethionine 65-71 histamine N-methyltransferase Homo sapiens 13-17 708699-0 1978 Affinity labeling of histamine N-methyltransferase by 2",3"-dialdehyde derivatives of S-adenosylhomocysteine and S-adenosylmethionine. S-Adenosylmethionine 113-133 histamine N-methyltransferase Homo sapiens 21-50 6343748-5 1983 The use of purified HNMT in the Hm assay has allowed the inclusion of high specific activity tritiated S-adenosyl-L-methionine ([3H]SAME) and the development of a simplified solvent extraction product isolation procedure. S-Adenosylmethionine 103-126 histamine N-methyltransferase Homo sapiens 20-24 3836703-3 1985 2.1.1.8; HMT) in the presence of the natural donor of methyl groups, [3H]-methyl-S-adenosyl-L-methionine ([3H]-SAMe). S-Adenosylmethionine 81-104 histamine N-methyltransferase Homo sapiens 9-12 907871-2 1977 Degradation of histamine by homogenized human skin in vitro, in the presence of the cofactor S-adenosyl methionine, indicates the presence of the histamine metabolizing enzyme histamine-N-methyl transferase in human skin. S-Adenosylmethionine 95-114 histamine N-methyltransferase Homo sapiens 176-206 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 histamine N-methyltransferase Homo sapiens 295-363 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 histamine N-methyltransferase Homo sapiens 295-363 1092359-7 1975 Its rate was low in the S-adenosylmethionine : N-acetylserotonin O-methyltransferase system (EC 2.1.1.4), and below recognition with S-adenosylmethionine : guanidinoacetate methyltransferase (EC 2.1.1.2) and S-adenosylmethionine : histamine N-methyltransferase (EC 2.1.1.8). S-Adenosylmethionine 26-44 histamine N-methyltransferase Homo sapiens 231-260