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 μM), of rat MAO B (K(i) = 2.9 ± 0.5 μM), and of zebrafish MAO (K(i) = 30.8 ± 5.3 μM). No inhibition is observed with purified human or rat MAO A. The 1.8 Å structure of the MAO B complex demonstrates that it binds within the substrate cavity.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Anticonvulsants / chemistry*
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Binding Sites
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Crystallography, X-Ray
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Humans
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Isoxazoles / chemistry*
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Models, Molecular
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Monoamine Oxidase / chemistry*
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Monoamine Oxidase Inhibitors / chemistry*
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Protein Binding
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Protein Conformation
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Rats
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Zonisamide
Substances
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Anticonvulsants
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Isoxazoles
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Monoamine Oxidase Inhibitors
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Zonisamide
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Monoamine Oxidase