Identification of N5,N10-methylene tetrahydrofolate reductase as the enzyme involved in the 5-methyl tetrahydrofolate-dependent formation of a beta-carboline derivative of 5-hydroxytryptamine in human platelets. |
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Authors: | R D Stebbins E Meller H Rosengarten A Friedhoff R Silber |
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Affiliation: | Departments of Medicine and Psychiatry, New York University School of Medicine, 550 First Avenue, New York, New York 10016 U.S.A. |
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Abstract: | An enzyme in human platelets or rat brain incubated with 5-methyl tetrahydrofolate (5MeH4folate) yields formaldehyde (4, 13), which will combine with biogenic amines to form β-carbolines (5) or tetrahydroisoquinolines. This activity was purified 500-fold from human platelets which are the main storage site for 5-hydroxytryptamine in man. This enzyme was identical to N5, N10-methylene tetrahydrofolate (N5,N10-methylene H4folate) reductase by the following criteria: (i) co-purification, (ii) heat denaturation, (iii) pH response, (iv) molecular weight, (5) cofactor requirements. A mechanism involving the enzymatic generation of formaldehyde followed by adduct formation with a biogenic amine is proposed. |
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Keywords: | To whom all correspondence should be addressed. |
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