Biology:Amine N-methyltransferase

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Short description: Class of enzymes


amine N-methyltransferase
INMT.jpeg
indolethylamine N-methyltransferase (with slight variation on CPK coloration) – See PDB 2A14
Identifiers
EC number2.1.1.49
CAS number51377-47-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / 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] 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]

The chemical reaction taking place is:

  • S-adenosyl-L-methionine + an amine [math]\displaystyle{ \rightleftharpoons }[/math] 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

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

See also

References

  1. 1.0 1.1 tryptamine+N-methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
  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" (in en). The FASEB Journal 29 (S1). doi:10.1096/fasebj.29.1_supplement.1022.7. ISSN 0892-6638. https://onlinelibrary.wiley.com/doi/10.1096/fasebj.29.1_supplement.1022.7. 
  3. 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. https://doi.org/10.1016/S0021-9258(18)68814-3. 
  4. 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. 

External links