Abstract
IT has been suggested that N-methylation of biogenic amines is involved in the development of certain schizophrenic disorders1,2. Interest in this transmethylation hypothesis has been boosted by the reported identification of a mammalian N-methyltransferase (“dopamine methyltransferase”3) which uses as methyl donor N5-methyltetrahydrofolate (MTHF) rather than S-adenosyl methionine3–5. Further studies have demonstrated that the products of the incubation of catecholamines or indoleamines with MTHF and the transferase were not N-methylated amines but tetrahydroisoquinoline or tetrahydro-β-carboline alkaloids, respectively6–10. These compounds can be formed readily by the condensation of formaldehyde with the amines and it has therefore been postulated that the enzyme originally identified as a methyltransferase may in fact act to release formaldehyde from MTHF6–10. We provide evidence that the enzyme methylenetetrahydrofolate reductase (EC 1.1.1.68) is responsible for the reported production of formaldehyde from MTHF.
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PEARSON, A., TURNER, A. Folate-dependent 1-carbon transfer to biogenic amines mediated by methylenetetrahydrofolate reductase. Nature 258, 173–174 (1975). https://doi.org/10.1038/258173a0
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DOI: https://doi.org/10.1038/258173a0
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