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  • Title: Beta-phenylethylamine and benzylamine as substrates for human monoamine oxidase A: A source of some anomalies?
    Author: Lewinsohn R, Glover V, Sandler M.
    Journal: Biochem Pharmacol; 1980 Mar 01; 29(5):777-81. PubMed ID: 20227955.
    Abstract:
    Monoamine oxidase (MAO) A predominates both in human placenta and lung. With 5-hydroxytryptamine (5-HT), beta-phenylethylamine (PEA) and benzylamine (Bz) as substrates and clorgyline and deprenyl, respectively, as selective MAO A and B inhibitors, their activity pattern has been defined and compared with that of human liver. PEA had a much higher V(max) with placental MAO A than did Bz; it behaved largely as an A substrate in placenta, and partly as an A substrate in lung. At commonly used substrate concentrations, deamination of Bz (sensitive to 10(-7) M deprenyl) was a better indicator of MAO B activity than deamination of PEA. The divergence between PEA and Bz as MAO A and B substrates may be one reason for some of the apparent discrepancies in the behaviour of MAO A and B noted in a variety of tissues in the literature. However, Bz reacts with benzylamine oxidase (BzAO) as well as MAO B. Depending on the tissue, deprenyl-resistant Bz activity may indicate the presence of BzAO rather than MAO A. As there is a widespread distribution of BzAO in man and rat, BzAO should be considered among the alternatives of enzyme activity when Bz is used as substrate.
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