Amine N-methyltransferase
(Redirected from INMT)
| amine N-methyltransferase | |||||||||
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 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 | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| INMT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | INMT, TEMT, indolethylamine N-methyltransferase | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 604854; MGI: 102963; GeneCards: INMT | |||||||||||||||||||||||||||||||||||||||||||||||||||||
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Amine N-methyltransferase (EC 2.1.1.49), also called indolethylamine N-methyltransferase, and thioether S-methyltransferase, is an enzyme that in humans is encoded by the INMT gene. It is ubiquitously present in non-neural tissues and catalyzes the N-methylation of tryptamine and structurally related compounds.[5][6] It can also catalyze the methylation of thioether and selenoether compounds, although the physiological significance of this biotransformation is not yet known.[7][8]
The general reaction taking place is:
- S-adenosyl-L-methionine + an amine S-adenosyl-L-homocysteine + a methylated amine
Function
[edit]Important reactions known to be catalysed by the enzyme include the dimethylation of tryptamine[9] and serotonin, which are transformed to N,N-dimethyltryptamine (DMT) and bufotenine respectively, for example:[10]
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.[6][11][12]
The enzyme can also transfer methyl groups to atoms other than nitrogen, for example sulfur and selenium.[7][8]
Nomenclature
[edit]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.[13]
Structural studies
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 2A14.
References
[edit]- 1 2 3 GRCh38: Ensembl release 89: ENSG00000241644 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000003477 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ 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.
- 1 2 tryptamine+N-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- 1 2 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.
- 1 2 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.
