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Author Notes:

CORRESPONDING AUTHOR: Dr. Dale E. Edmondson, Department of Biochemistry, Rollins Research Bldg. 1510 Clifton Rd., Atlanta, Georgia, 30322 USA. deedmon@emory.edu; Phone : 404-727-5972; Fax: 404-727-2738


Research Funding:

National Institute of General Medical Sciences : NIGMS

This work was supported by grants from Fondazione Bussolera, Fondazione Cariplo and the National Institute of General Medical Sciences (GM-29433).


  • Zonisamide
  • human monoamine oxidase B
  • crystal structure
  • competitive inhibition

Interactions of Monoamine Oxidases with the Antiepileptic Drug Zonisamide: Specificity of Inhibition and Structure of the Human Monoamine oxidase B Complex


Journal Title:

Journal of Medicinal Chemistry


Volume 54, Number 3


, Pages 909-912

Type of Work:

Article | Post-print: After Peer Review


The binding of zonisamide to purified, recombinant monoamine oxidases (MAOs) has been investigated. It is a competitive inhibitor of human MAO B (Ki = 3.1 ± 0.3 μM), of rat MAO B (Ki = 2.9 ± 0.5 μM), and of zebrafish MAO (Ki = 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.

Copyright information:

© 2010 American Chemical Society

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