Enzymatic Formation of Psychotomimetic Metabolites from Normally Occurring Compounds

  title={Enzymatic Formation of Psychotomimetic Metabolites from Normally Occurring Compounds},
  author={Julius Axelrod},
  pages={343 - 343}
  • J. Axelrod
  • Published 4 August 1961
  • Chemistry, Biology
  • Science
An enzyme has been found that N-methylates serotonin and tryptamine to psychotomimetic metabolites, bufotenine and N,N-dimethyltryptamine. This enzyme is highly localized in the rabbit lung and also N-methylates phenylethylamine derivatives such as tyramine, phenylethylamine , mescaline, and dopamine. 
Psychotomimetic N-Methylated Tryptamines: Formation in Brain in vivo and in vitro
An enzyme that converts tryptamine and N-methyl-tryptamine to N- methyl-and dimethyltryptamine was found to be present in rat and human brain.
Methyltetrahydrofolic Acid Mediates N- and O-Methylation of Biogenic Amines
With methyltetrahydrofolic acid, serotonin is O-methylated to 5-methoxytryptamine, a novel indoleamine in mammalian brain.
Tryptoline formation by a preparation from brain with 5-methyltetrahydrofolic acid and tryptamine.
An enzymatic preparation from human brain converts tryptamine to tryptoline (9H-1,2,3, 4-tetrahydropyrido[3,4-b]indole) and N-methyltryptamine and 5-hydroxytryptamine yield 1-mthyltryptoline and 5,hydroxyTryptoline, respectively.
Indole(ethyl)amine N-methyltransferase in human brain.
Preliminary evidence gathered in laboratories from rats infused intraventricularly with bufotenin has suggested that this substance is at least as potent as its powerfully hallucinogenic 5-methoxy congener, and may not easily cross the blood-brain barrier.
N, N-dimethyltryptamine: an endogenous hallucinogen.
When the Endogenous Hallucinogenic Trace Amine N,N-Dimethyltryptamine Meets the Sigma-1 Receptor
This work presents a hypothetical signaling scheme that might be triggered by the binding of DMT to sigma-1 receptors, which are ligand-regulated molecular chaperones whose function includes inhibiting various voltage-sensitive ion channels.


A report on the assay, purification, properties, and distribution of this enzyme is in preparation