Amine N-methyltransferase
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.[1] More recently, it was discovered that this enzyme can also catalyze the methylation of thioether and selenoether compounds, although the physiological significance of this biotransformation is not yet known.[2][3]
| 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 |
The chemical reaction taking place is:
- S-adenosyl-L-methionine + an amine 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. In the case of tryptamine and serotonin these then become the dimethylated indolethylamines N,N-dimethyltryptamine (DMT) and bufotenine respectively.[4]
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. This enzyme participates in tryptophan metabolism.
A wide range of primary, secondary and tertiary amines can act as acceptors, including tryptamine, aniline, nicotine and a variety of drugs and other xenobiotics.[1]
Structural studies edit
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2A14.
See also edit
References edit
- ^ a b 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). 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.
- ^ 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.
- Ansher SS, Jakoby WB (1986). "Amine N-methyltransferases from rabbit liver". J. Biol. Chem. 261 (9): 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 (9): 1673–7. doi:10.1016/0006-2952(88)90426-1. PMID 3377829.
External links edit
- EC 2.1.1.49
- Lyon ES, Jakoby WB (1981). "Arylamine N-methyltransferase". Meth. Enzymol. Methods in Enzymology. 77: 263–6. doi:10.1016/S0076-6879(81)77035-6. ISBN 9780121819774. PMID 6276654.
- 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.