Nicotinate N-methyltransferase
nicotinate N-methyltransferase | |||||||||
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![]() HhaI methyltransferase monomer + DNA fragment, Haemophilus haemolyticus | |||||||||
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 | ||||||||
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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 .
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. PMID 13790768.
- EC 2.1.1
- Enzymes of known structure
- EC 2.1 stubs