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l-Deprenyl: A Unique MAO-B Inhibitor

  • E. E. Polymeropoulos
Part of the Milestones in Drug Therapy book series (MDT)

Abstract

Monoamine oxidase (MAO) is a flavin-adenosine-dinucleotide (FAD) — containing enzyme located on the outer mitochondrial membrane [1–3]. Its function is to catalyze the oxidative deamination of biogenic amines to the corresponding aldehyde [4]. It is generally accepted that it exists in two functional isoenzyme forms, MAO-A and MAO-B, each of which shows preferential affinity for substrates and specificity towards inhibitors [3, 5]. Available evidence suggests that two different proteins are responsible for the activity of the isoenzymes [6–8]. Although the role of the FAD cofactor in the oxidative process seems to be quite clear, the position of FAD relative to the substrate recognition and binding site has not yet been resolved. However, the structure of the flavin peptide has been determined, and it has been shown that for the liver and brain enzymes FAD is covalently linked at the 8a-carbon atom of the isoalloxazine ring to a cystein via a thioether bridge [9]. The sequence of the peptide together with the bound flavin is shown in Figure 1.

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© Springer Basel AG 1993

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  • E. E. Polymeropoulos

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