Reaction participants Show >> << Hide
- Name help_outline a secondary amine Identifier CHEBI:137419 Charge 1 Formula H2NR2 SMILEShelp_outline *[NH+](*)[H] 2D coordinates Mol file for the small molecule Search links Involved in 35 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-methionine Identifier CHEBI:59789 Charge 1 Formula C15H23N6O5S InChIKeyhelp_outline MEFKEPWMEQBLKI-AIRLBKTGSA-O SMILEShelp_outline C[S+](CC[C@H]([NH3+])C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 842 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a methylated secondary amine Identifier CHEBI:137984 Charge 1 Formula CH4NR2 SMILEShelp_outline *[NH+](*)C 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline S-adenosyl-L-homocysteine Identifier CHEBI:57856 Charge 0 Formula C14H20N6O5S InChIKeyhelp_outline ZJUKTBDSGOFHSH-WFMPWKQPSA-N SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](CSCC[C@H]([NH3+])C([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 768 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:53924 | RHEA:53925 | RHEA:53926 | RHEA:53927 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Amine N-methyltransferases from rabbit liver.
Ansher S.S., Jakoby W.B.
N-Methylation of amines has been ascribed to enzymes listed as amine N-methyltransferase, indolethylamine N-methyltransferase, and arylamine N-methyltransferase. All of these activities are accomplished by each of two related enzymes present in rabbit liver. The two N-methyltransferases have a ver ... >> More
N-Methylation of amines has been ascribed to enzymes listed as amine N-methyltransferase, indolethylamine N-methyltransferase, and arylamine N-methyltransferase. All of these activities are accomplished by each of two related enzymes present in rabbit liver. The two N-methyltransferases have a very broad and overlapping specificity for primary and secondary amines. Both have a molecular mass of 30,000 daltons and react with an antibody formed to one of them, but have different isoelectric points. << Less
J Biol Chem 261:3996-4001(1986) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Formation of quaternary amines by N-methylation of azaheterocycles with homogeneous amine N-methyltransferases.
Crooks P.A., Godin C.S., Damani L.A., Ansher S.S., Jakoby W.B.
Catalytic activities of two amine N-methyltransferases were documented for the following azaheterocycles: isomeric phenyl- and bispyridyls; 2-, 3- and 4-mono-substituted pyridines; and a miscellaneous group of azaheterocycles that included mono- and diazabenzenes and mono- and diazanaphthalenes. T ... >> More
Catalytic activities of two amine N-methyltransferases were documented for the following azaheterocycles: isomeric phenyl- and bispyridyls; 2-, 3- and 4-mono-substituted pyridines; and a miscellaneous group of azaheterocycles that included mono- and diazabenzenes and mono- and diazanaphthalenes. The broad substrate specificities of the two amine N-methyltransferases for primary and secondary amines are here extended to a large number of aromatic azaheterocycles in which N-methylation results in the formation of quaternary ammonium metabolites. Pyridine was the best substrate for both enzymes. Substitution in the ring at the 2-position sterically hindered methylation of the pyridyl nitrogen; 2-phenylpyridine and 2,2'-bispyridyl were not substrates. << Less
Biochem Pharmacol 37:1673-1677(1988) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism.
Mozier N.M., McConnell K.P., Hoffman J.L.
The final urinary excretion product of selenium detoxification is trimethylselenonium ion. An assay has been developed for the enzyme, S-adenosylmethionine:thioether S-methyltransferase, responsible for this final methylation reaction. This assay employed high pressure liquid chromatography separa ... >> More
The final urinary excretion product of selenium detoxification is trimethylselenonium ion. An assay has been developed for the enzyme, S-adenosylmethionine:thioether S-methyltransferase, responsible for this final methylation reaction. This assay employed high pressure liquid chromatography separation and quantitation of the trimethylselenonium ion produced by thioether methyltransferase acting on S-adenosylmethionine and dimethyl selenide. The enzyme was shown to reside primarily in the cytosol of mouse lung (30 pmol/mg protein/min) and liver (7 pmol/mg protein/min). Purification from mouse lung to a preparation that exhibited a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was achieved by DEAE, gel filtration, and chromatofocusing chromatographies. Thioether methyltransferase is monomeric with a molecular weight of 28,000 and has a pI of 5.3. The pH optimum was 6.3, and Km values for dimethyl selenide and S-adenosylmethionine were 0.4 and 1.0 microM, respectively. The enzyme was inhibited 50% by 25 microM sinefungin, an analog of S-adenosylmethionine, or 40 microM S-adenosylhomocysteine, the reaction product. Pure thioether methyltransferase methylated selenium in dimethyl selenide, tellurium in dimethyl telluride, and S in dimethyl sulfide and many other thioethers. These data suggest a general role for this novel enzyme in the synthesis of onium compounds with increased aqueous solubility helpful in their excretion. << Less
J. Biol. Chem. 263:4527-4531(1988) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.