Nicotinate N-methyltransferase
| nicotinate N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.7 | ||||||||
| CAS no. | 9029-79-2 | ||||||||
| 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 nicotinate N-methyltransferase (EC 2.1.1.7) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + nicotinate S-adenosyl-L-homocysteine + N-methylnicotinate
Thus, the two substrates of this enzyme are S-adenosyl methionine and nicotinate, whereas its two products are S-adenosylhomocysteine and N-methylnicotinate.
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:nicotinate N-methyltransferase. Other names in common use include furanocoumarin 8-methyltransferase, and furanocoumarin 8-O-methyltransferase. This enzyme participates in nicotinate and nicotinamide metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 5MHT.
References
- Joshi JG, Handler P (1960). "Biosynthesis of trigonelline". J. Biol. Chem. 235: 2981–2983.
