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

被引：52

作者：

Binda, Claudia ^{[2
]}

Aldeco, Milagros ^{[1
]}

Mattevi, Andrea ^{[2
]}

Edmondson, Dale E. ^{[1
]}

机构：

[1] Emory Univ, Sch Med, Dept Biochem, Atlanta, GA 30322 USA

[2] Univ Pavia, Dept Genet & Microbiol, I-27100 Pavia, Italy

来源：

JOURNAL OF MEDICINAL CHEMISTRY | 2011年 / 54卷 / 03期

关键词：

HIGH-LEVEL EXPRESSION; PICHIA-PASTORIS; HUMAN-MAO; PARKINSONS-DISEASE; ANTICONVULSANT; PURIFICATION; RESOLUTION; MPTP;

D O I：

10.1021/jm101359c

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

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 mu M), of rat MAO B (K-i = 2.9 +/- 0.5 mu M), and of zebrafish MAO (K-i = 30.8 +/- 5.3 mu M). No inhibition is observed with purified human or rat MAO A. The 1.8 angstrom structure of the MAO B complex demonstrates that it binds within the substrate cavity.

引用

页码：909 / 912

页数：4

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