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A new metabolic pathway for N,N-dimethyltryptamine.

L M Hryhorczuk, J M Rainey, C E Frohman

    Biological Psychiatry
    |January 1, 1986
    PubMed
    Summary
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    N,N-Dimethyltryptamine (DMT) is converted to dimethylkynuramine (DMK) in human blood. This structural change, identified via HPLC, is catalyzed by an unknown enzyme, distinct from known dioxygenases.

    Area of Science:

    • Biochemistry
    • Pharmacology
    • Toxicology

    Background:

    • N,N-Dimethyltryptamine (DMT) is a psychoactive compound found in various organisms.
    • The metabolic fate of DMT in human blood has not been fully elucidated.
    • Understanding DMT metabolism is crucial for pharmacology and toxicology.

    Purpose of the Study:

    • To investigate the in vitro metabolic transformation of N,N-Dimethyltryptamine (DMT) in whole human blood and red blood cells.
    • To identify the primary metabolite of DMT in this biological matrix.
    • To characterize the enzymatic activity responsible for DMT transformation.

    Main Methods:

    • Incubation of DMT with whole human blood and isolated red blood cells.
    • Analysis of reaction products using high-pressure liquid chromatography (HPLC).

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  • Identification of the metabolite using ultraviolet spectrophotometry and mass spectrometry.

    • Main Results:

    • DMT undergoes a significant structural alteration in human blood and red blood cells.
    • A novel high-pressure liquid chromatography (HPLC) peak corresponding to dimethylkynuramine (DMK) was observed.
    • Mass spectrometry and ultraviolet spectrophotometry confirmed the identity of the metabolite as DMK.
    • The enzyme responsible for DMK formation appears distinct from tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase.

    Conclusions:

    • N,N-Dimethyltryptamine (DMT) is rapidly metabolized to dimethylkynuramine (DMK) in human blood.
    • This transformation is mediated by an unidentified enzymatic activity within red blood cells.
    • Further research is needed to identify the specific enzyme and its physiological role.