Amine N-methyltransferase

From Wikipedia, the free encyclopedia

In enzymology, an amine N-methyltransferase (EC 2.1.1.49) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + an amine $\rightleftharpoons$ S-adenosyl-L-homocysteine + a methylated amine

Thus, the two substrates of this enzyme are S-adenosyl methionine and amine, whereas its two products are S-adenosylhomocysteine and methylated amine.

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:amine N-methyltransferase. Other names in common use include nicotine N-methyltransferase, tryptamine N-methyltransferase, arylamine N-methyltransferase, and tryptamine methyltransferase. This enzyme participates in tryptophan metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2A14.

[edit] References

IUBMB entry for 2.1.1.49
BRENDA references for 2.1.1.49 (Recommended.)
PubMed references for 2.1.1.49
PubMed Central references for 2.1.1.49
Google Scholar references for 2.1.1.49
Ansher SS, Jakoby WB (1986). "Amine N-methyltransferases from rabbit liver". J. Biol. Chem. 261: 3996–4001. PMID 3949799.
Crooks PA, Godin CS, Damani LA, Ansher SS, Jakoby WB (1988). "Formation of quaternary amines by N-methylation of azaheterocycles with homogeneous amine N-methyltransferases". Biochem. Pharmacol. 37: 1673–7. doi:10.1016/0006-2952(88)90426-1. PMID 3377829.