Biology:Amine N-methyltransferase
| amine N-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 indolethylamine N-methyltransferase (with slight variation on CPK coloration) – See PDB 2A14 | |||||||||
| Identifiers | |||||||||
| EC number | 2.1.1.49 | ||||||||
| CAS number | 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.[1][2] It can also catalyze the methylation of thioether and selenoether compounds, although the physiological significance of this biotransformation is not yet known.[3][4]
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 tryptamine[5] and serotonin, which are transformed to N,N-dimethyltryptamine (DMT) and bufotenine respectively, for example:[6]
- REDIRECT Template:Chemical reaction
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.[2][7][8]
The enzyme can also transfer methyl groups to atoms other than nitrogen, for example sulfur and selenium.[3][4]
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
- ↑ "Amine N-methyltransferases from rabbit liver". J. Biol. Chem. 261 (9): 3996–4001. 1986. doi:10.1016/S0021-9258(17)35612-0. PMID 3949799.
- ↑ 2.0 2.1 tryptamine+N-methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
- ↑ 3.0 3.1 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" (in en). The FASEB Journal 29 (S1). doi:10.1096/fasebj.29.1_supplement.1022.7. ISSN 0892-6638.
- ↑ 4.0 4.1 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.
- ↑ "Tryptamine-N-methyltransferase activity in brain tissue: a re-examination". Brain Res. 114 (2): 359–64. 1976. doi:10.1016/0006-8993(76)90680-6. PMID 963555.
- ↑ J., Kärkkäinen; T. Forsström; J. Tornaeus; K. Wähälä; P. Kiuru; A. Honkanen; U. -H. Stenman; U. Turpeinen et al. (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.
- ↑ "Arylamine N-methyltransferase". Detoxication and Drug Metabolism: Conjugation and Related Systems. Methods in Enzymology. 77. 1981. pp. 263–6. doi:10.1016/S0076-6879(81)77035-6. ISBN 9780121819774.
- ↑ "Formation of quaternary amines by N-methylation of azaheterocycles with homogeneous amine N-methyltransferases". Biochem. Pharmacol. 37 (9): 1673–7. 1988. doi:10.1016/0006-2952(88)90426-1. PMID 3377829. https://zenodo.org/record/1253816.
- ↑ Enzyme 2.1.1.49 at KEGG Pathway Database.
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