title: Interactions of monoamine oxidases with the antiepileptic drug zonisamide: specificity of inhibition and structure of the human monoamine oxidase B complex.
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.
authors.affiliation: Department Genetics and Microbiology, University of Pavia, via Ferrata 1, Pavia 27100, Italy.
authors.forename: Claudia
authors.initials: C
authors.lastname: Binda
authors.forename: Milagros
authors.initials: M
authors.lastname: Aldeco
authors.forename: Andrea
authors.initials: A
authors.lastname: Mattevi
authors.forename: Dale E
authors.initials: DE
authors.lastname: Edmondson
mesh_terms: D000818:Animals; D000927:Anticonvulsants / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006801:Humans; D007555:Isoxazoles / Q000737:chemistry*; D008958:Models, Molecular; D008995:Monoamine Oxidase / Q000737:chemistry*; D008996:Monoamine Oxidase Inhibitors / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D000078305:Zonisamide
chemical_list: D000927:Anticonvulsants; D007555:Isoxazoles; D008996:Monoamine Oxidase Inhibitors; D000078305:Zonisamide; D008995:Monoamine Oxidase