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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ABSTRACT:
SUBMITTER: Binda C
PROVIDER: S-EPMC3071873 | biostudies-literature | 2011 Feb
REPOSITORIES: biostudies-literature
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Interactions of monoamine oxidases with the antiepileptic drug zonisamide: specificity of inhibition and structure of the human monoamine oxidase B complex.
Binda Claudia C Aldeco Milagros M Mattevi Andrea A Edmondson Dale E DE
Journal of medicinal chemistry 20101222 3
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. ...[more]
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