| amine N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 indolethylamine N-methyltransferase (with slight variation on CPK coloration) – See PDB 2A14 | |||||||||
| Identifiers | |||||||||
| EC no. | 2.1.1.49 | ||||||||
| CAS no. | 51377-47-0 | ||||||||
| 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 | ||||||||
| |||||||||
Amine N-methyltransferase (EC 2.1.1.49), also called indolethylamine N-methyltransferase, and thioether S-methyltransferase, is an enzyme that is ubiquitously present in non-neural tissues and catalyzes the N-methylation of tryptamine and structurally related compounds.12 It can also catalyze the methylation of thioether and selenoether compounds, although the physiological significance of this biotransformation is not yet known.34
The general reaction taking place is:
- S-adenosyl-L-methionine + an amine S-adenosyl-L-homocysteine + a methylated amine
Function
Important reactions known to be catalysed by the enzyme include the dimethylation of tryptamine5 and serotonin, which are transformed to N,N-dimethyltryptamine (DMT) and bufotenine respectively, for example:6
A wide range of primary, secondary and tertiary amines can act as substrates, including tryptamine, aniline, nicotine and a variety of drugs and other xenobiotics.278
The enzyme can also transfer methyl groups to atoms other than nitrogen, for example sulfur and selenium.34
Nomenclature
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, indolethylamine N-methyltransferase, and arylamine N-methyltransferase.9
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2A14.
References
References
- Ansher SS, Jakoby WB (1986). "Amine N-methyltransferases from rabbit liver". J. Biol. Chem. 261 (9): 3996–4001. doi:10.1016/S0021-9258(17)35612-0. PMID 3949799.
- tryptamine+N-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Chu, Uyen; Mavlyutov, Timur; Schulman, Amanda; Baker, Erin; Raj, Rebecca; Epstein, Miles; Guo, Lian; Ruoho, Arnold (April 2015). "Methylation of Thiols and Thioethers by Human Indolethylamine-N Methyl Transferase". The FASEB Journal. 29 (S1) 1022.7. doi:10.1096/fasebj.29.1_supplement.1022.7. ISSN 0892-6638.
- Mozier, N M; McConnell, K P; Hoffman, J L (April 1988). "S-adenosyl-L-methionine:thioether S-methyltransferase, a new enzyme in sulfur and selenium metabolism". Journal of Biological Chemistry. 263 (10): 4527–4531. doi:10.1016/s0021-9258(18)68814-3. ISSN 0021-9258. PMID 3350800.
- Boarder MR, Rodnight R (1976). "Tryptamine-N-methyltransferase activity in brain tissue: a re-examination". Brain Res. 114 (2): 359–64. doi:10.1016/0006-8993(76)90680-6. PMID 963555. S2CID 36334101.
- J., Kärkkäinen; T. Forsström; J. Tornaeus; K. Wähälä; P. Kiuru; A. Honkanen; U. -H. Stenman; U. Turpeinen; A. Hesso (April 2005). "Potentially hallucinogenic 5-hydroxytryptamine receptor ligands bufotenine and dimethyltryptamine in blood and tissues". Scandinavian Journal of Clinical and Laboratory Investigation. 65 (3): 189–199. doi:10.1080/00365510510013604. PMID 16095048. S2CID 20005294.
- Lyon ES, Jakoby WB (1981). "Arylamine N-methyltransferase". Detoxication and Drug Metabolism: Conjugation and Related Systems. Methods in Enzymology. Vol. 77. pp. 263–6. doi:10.1016/S0076-6879(81)77035-6. ISBN 9780121819774. PMID 6276654.
- 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 (9): 1673–7. doi:10.1016/0006-2952(88)90426-1. PMID 3377829.
- Enzyme 2.1.1.49 at KEGG Pathway Database.