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Nicotinate N-methyltransferase

From Wikipedia, the free encyclopedia
nicotinate N-methyltransferase
HhaI methyltransferase monomer + DNA fragment, Haemophilus haemolyticus
Identifiers
EC no.2.1.1.7
CAS no.9029-79-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

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

References

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  • 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.