Nicotinate N-methyltransferase
| Nicotinate N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 HhaI methyltransferase monomer + DNA fragment, Haemophilus haemolyticus | |||||||||
| Identifiers | |||||||||
| EC no. | 2.1.1.7 | ||||||||
| CAS no. | 9029-79-2 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Nicotinate N-methyltransferase (EC 2.1.1.7) is an enzyme that catalyzes the chemical reaction
The enzyme catalyses a methylation reaction in which nicotinic acid is converted to trigonelline (N-methylnicotinate). The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which loses its methyl group and becomes S-adenosyl-L-homocysteine (SAH).[1]
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.[2]
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 5MHT.
References
- ↑ Joshi JG, Handler P (1960). "Biosynthesis of trigonelline". J. Biol. Chem. 235 (10): 2981–2983. doi:10.1016/S0021-9258(18)64575-2. PMID 13790768.
- ↑ Enzyme 2.1.1.7 at KEGG Pathway Database.
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