Amine N-methyltransferase explained

amine N-methyltransferase
Ec Number:2.1.1.49
Cas Number:51377-47-0
Go Code:0030748

Amine N-methyltransferase, 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. 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.[1] [2]

The chemical reaction taking place is:

\rightleftharpoons

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.[3]

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.

Structural studies

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

See also

References

External links

Notes and References

  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 . The FASEB Journal . en . 29 . S1 . 10.1096/fasebj.29.1_supplement.1022.7 . free . 0892-6638.
  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 . 10.1016/s0021-9258(18)68814-3 . 0021-9258. free . 3350800 .
  3. 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 . 10.1080/00365510510013604 . 16095048 . 20005294 .