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Inhibition of Monoamine Oxidase by Evodiamine  

Lee, Sang-Seon (College of Pharmacy, and Research Center for Bioresource and Health, Chungbuk National University)
Hwang, Bang-Yeon (College of Pharmacy, and Research Center for Bioresource and Health, Chungbuk National University)
Ro, Jai-Seup (College of Pharmacy, and Research Center for Bioresource and Health, Chungbuk National University)
Lee, Myung-Koo (College of Pharmacy, and Research Center for Bioresource and Health, Chungbuk National University)
Publication Information
Korean Journal of Pharmacognosy / v.37, no.4, 2006 , pp. 320-323 More about this Journal
Abstract
The effects of evodiamine on monoamine oxidase (MAO) activity were investigated. MAO was purified from mouse brain and the $K_m\;and\;V_{max}$ values of MAO were $78.5{\pm}5.28{\mu}M$ and $0.68{\pm}0.07$ nmol/min/mg protein, respectively (n=4). Evodiamine at $30-120{\mu}M$ showed an inhibitory effect on MAO activity using a substrate kynuramine with an $IC_{50}$ value of $104.2{\mu}M$ (n=4). Evodiamine also exhibited a non-competitive inhibition on MAO. The $K_i$ value for evodiamine was $72.5{\pm}10.8{\mu}M$ (n=4). These results suggest that evodiamine partially contributes to the regulation of monoamine content.
Keywords
evodiamine; monoamine oxidase; mouse brain; kynuramine; non-competitive inhibition;
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