Enzymes
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- Name help_outline pyridine Identifier CHEBI:16227 (Beilstein: 103233; CAS: 110-86-1) help_outline Charge 0 Formula C5H5N InChIKeyhelp_outline JUJWROOIHBZHMG-UHFFFAOYSA-N SMILEShelp_outline c1ccncc1 2D coordinates Mol file for the small molecule Search links Involved in 3 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 868 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-methylpyridinium Identifier CHEBI:15761 (CAS: 694-56-4) help_outline Charge 1 Formula C6H8N InChIKeyhelp_outline PQBAWAQIRZIWIV-UHFFFAOYSA-N SMILEShelp_outline C[n+]1ccccc1 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 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 792 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:16893 | RHEA:16894 | RHEA:16895 | RHEA:16896 | |
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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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N-methylation and quaternization of pyridine in vitro by rabbit lung, liver and kidney N-methyltransferases: an S-adenosyl-L-methionine-dependent reaction.
Damani L.A., Shaker M.S., Crooks P.A., Godin C.S., Nwosu C.
The N-methylation of pyridine in vitro, using dialysed and undialysed hepatic, pulmonary, renal and brain preparations from rabbits, is described. Analysis of the quaternary metabolite, N-methylpyridinium ion, was carried out by selective ion-pair extraction and cation-exchange high-performance li ... >> More
The N-methylation of pyridine in vitro, using dialysed and undialysed hepatic, pulmonary, renal and brain preparations from rabbits, is described. Analysis of the quaternary metabolite, N-methylpyridinium ion, was carried out by selective ion-pair extraction and cation-exchange high-performance liquid chromatography (h.p.l.c.) using a u.v. detector, and also by direct cation-exchange h.p.l.c. of incubates containing S-adenosyl-L-[methyl-3H]methionine using a flow-through radioactivity detector. N-Methylation of pyridine could be readily demonstrated with dialysed homogenates, 9000 g and 100 000 g supernatant fractions from lung, kidney and liver, but not with any of the brain preparations. 'Pyridine N-methyltransferase' activity was confined to the tissue cytosol, and this enzyme utilized S-adenosyl-L-methionine as the methyl donor. Since the activity of the 'pyridine N-methyltransferase' in rabbit tissues is increased many fold by dialysis, this enzyme, in common with most other N-methylating enzymes, is subject to inhibition by a low-molecular-weight endogenous substance. << Less