| pyridine N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.87 | ||||||||
| CAS no. | 104327-10-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a pyridine N-methyltransferase (EC 2.1.1.87) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + pyridine S-adenosyl-L-homocysteine + N-methylpyridinium
Thus, the two substrates of this enzyme are S-adenosyl methionine and pyridine, whereas its two products are S-adenosylhomocysteine and N-methylpyridinium.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:pyridine N-methyltransferase. This enzyme is also called pyridine methyltransferase.
References
- Damani LA, Shaker MS, Crooks PA, Godin CS, Nwosu C (1986). "N-methylation and quaternization of pyridine in vitro by rabbit lung, liver and kidney N-methyltransferases: an S-adenosyl-L-methionine-dependent reaction". Xenobiotica. 16 (7): 645–50. doi:10.3109/00498258609043554. PMID 3751119.
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