Both MAO enzymes have a substrate-binding cavity and an entrance cavity in which the substrate-binding sites are hydrophobic and are enclosed with aromatic and aliphatic residues. 10 In human MAO-A, the substrate-binding site is a 400 3 cavity, but in MAO-B, a smaller lipophilic cavity, called the entry cavity, sits between the main
The efficacy of the inhibitor binding into the unique substrate binding sites of MAO-A and MAO-B ultimately determines a drug s relative selectivity at inhibiting MAO-A, MAO-B, or both. The substrate binding sites of both MAO-A and MAO-B are mainly hydrophobic except for a conserved lysine that interacts with a water molecule.
The effects of small daily doses of MAOI are therefore cumulative. The biochemical effects of these drugs will involve several substrates of MAO, e.g. dopamine
Avoid concomitant use with drugs that enhance serotonergic transmission (e.g, SSRIs, SNRIs, MAO inhibitors). Substrate for P
The efficacy of the inhibitor binding into the unique substrate binding sites of MAO-A and MAO-B ultimately determines a drug s relative selectivity at inhibiting MAO-A, MAO-B, or both. The substrate binding sites of both MAO-A and MAO-B are mainly hydrophobic except for a conserved lysine that interacts with a water molecule.
The efficacy of the inhibitor binding into the unique substrate binding sites of MAO-A and MAO-B ultimately determines a drug s relative selectivity at inhibiting MAO-A, MAO-B, or both. The substrate binding sites of both MAO-A and MAO-B are mainly hydrophobic except for a conserved lysine that interacts with a water molecule.
Dopamine is a substrate for both MAO-A and MAO-B, so selective MAO-B inhibitors are used to manage Parkinson's disease. The MAOIs can be
ant8,9 and anxiolytic drugs,10,11 whereas MAO-B inhibitors are used for the treatment of Parkinson s12,13 and Alzheimer s diseases.7 In contrast, a limited number of MAO substrates have been reported: Kynuramine14 (Fig. 1), a metabolite of melatonin,15 is a substrate for both MAO-A and B and used in in vitro MAO
Tyramine was the first known substrate for MAO, which had initially been referred to as tyramine oxidase, and may still today be a suitable in vivo probe drug for studying MAO activity. Although tyramine is a substrate of both MAO-A and MAO-B, the tyramine pressor response occurs only with MAO-A inhibition ( Finberg and Tenne, 2024 ; Finberg
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