Nicotinate N-methyltransferase
From Wikipedia, the free encyclopedia
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.
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[edit] Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 5MHT.
[edit] References
- IUBMB entry for 2.1.1.7
- BRENDA references for 2.1.1.7 (Recommended.)
- PubMed references for 2.1.1.7
- PubMed Central references for 2.1.1.7
- Google Scholar references for 2.1.1.7
- Joshi JG and Handler P (1960). "Biosynthesis of trigonelline". J. Biol. Chem. 235: 2981–2983.
[edit] External links
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- The CAS registry number for this enzyme class is 9029-79-2.

