Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 50, Issue 23, Pages 5848-5852Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jm070677y
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- NIGMS NIH HHS [GM-29433] Funding Source: Medline
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Structures of human monoamine oxidase B (MAO B) in complex with safinamide and two coumarin derivatives, all sharing a common benzyloxy substituent, were determined by X-ray crystallography. These compounds competitively inhibit MAO B with K-i values in the 0.1-0.5 mu M range that are 30-700-fold lower than those observed with MAO A. The inhibitors bind noncovalently to MAO B, occupying both the entrance and the substrate cavities and showing a similarly oriented benzyloxy substituent.
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