Abstract
Monoamine oxidase (MAO, E.C. 1.4.3.4.), which has been shown to exist in two forms (termed A and B), plays an essential role in the metabolism of tyramine and of 2-phenylethylamine (PEA). The two forms of the enzyme are defined according to their sensitivity to clorgyline; the A-form being highly sensitive and the B-form less sensitive. In contrast to clorgyline, FLA 336(+) is a reversible MAO-A inhibitor (1), while (−)deprenyl is an irreversible inhibitor with a high specificity for the MAO-B form (2). In most tissues tyramine is an equally well preferred substrate for both forms of the enzyme, while PEA is mainly a substrate for the B-form (3).
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Oreland, L., Lundberg, PA., Engberg, G. (1985). Central Effects of Tyramine and PEA. In: Boulton, A.A., Maitre, L., Bieck, P.R., Riederer, P. (eds) Neuropsychopharmacology of the Trace Amines. Humana Press. https://doi.org/10.1007/978-1-4612-5010-4_19
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DOI: https://doi.org/10.1007/978-1-4612-5010-4_19
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