Interactions of monoamine oxidases with the antiepileptic drug zonisamide: specificity of inhibition and structure of the human monoamine oxidase B complex.

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Binda C, Aldeco M, Mattevi A, Edmondson DE

Interactions of monoamine oxidases with the antiepileptic drug zonisamide: specificity of inhibition and structure of the human monoamine oxidase B complex.

J Med Chem. 2011 Feb 10;54(3):909-12. doi: 10.1021/jm101359c. Epub 2010 Dec 22.

PubMed ID

21175212 [ View in PubMed

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Abstract

The binding of zonisamide to purified, recombinant monoamine oxidases (MAOs) has been investigated. It is a competitive inhibitor of human MAO B (K(i) = 3.1 +/- 0.3 muM), of rat MAO B (K(i) = 2.9 +/- 0.5 muM), and of zebrafish MAO (K(i) = 30.8 +/- 5.3 muM). No inhibition is observed with purified human or rat MAO A. The 1.8 A structure of the MAO B complex demonstrates that it binds within the substrate cavity.

DrugBank Data that Cites this Article

Binding Properties

Drug	Target	Property	Measurement	pH	Temperature (°C)
Zonisamide	Amine oxidase [flavin-containing] B	Ki (nM)	3100	N/A	N/A	Details