Nicotinate N-methyltransferase

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
nicotinate N-methyltransferase
Identifiers
EC number2.1.1.7
CAS number9029-79-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / 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[edit]

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 5MHT.

References[edit]

  • Joshi JG, Handler P (1960). "Biosynthesis of trigonelline". J. Biol. Chem. 235: 2981–2983.