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Indolethylamine N-methyltransferase (INMT) is a methyltransferase enzyme that catalyzes the transfer of methyl groups from S-adenosyl-L-methionine (SAM) to the amino groups of small molecules, mainly indolethylamines such as tryptamine, and structurally related compounds[1][2][3]. INMT is most recognized for its role in the biosynthesis of N,N-dimethyltryptamine (DMT), a compound with psychotropic effects, through double methylation of tryptamine. It is expressed in multiple human and mammalian tissues, primarily non-neural, and also contributes to detoxification pathways via methylation of thioether, selenoether, and related compounds[2][3]. The gene displays significant species differences in its activity and substrate specificity (notably, rat INMT does not catalyze DMT biosynthesis under usual conditions)[1]. Disruption or polymorphisms in INMT may be implicated in disease processes such as hallucinogen response and nephrolithiasis, but its full physiological and pathological roles remain under investigation.
Methylation of amine substrates (notably tryptamine, aniline, nicotine); Detoxification reactions (e.g., methylation of selenium and thioether compounds)[2][3]
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