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

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

Author information

1
Department Genetics and Microbiology, University of Pavia, via Ferrata 1, Pavia 27100, Italy.

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.

PMID:
21175212
PMCID:
PMC3071873
DOI:
10.1021/jm101359c
[Indexed for MEDLINE]
Free PMC Article

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