| Literature DB >> 12672993 |
Myung Koo Lee1, Bang Yeon Hwang, Seon A Lee, Gab Jin Oh, Woo Hoi Choi, Seong Su Hong, Kyong Soon Lee, Jai Seup Ro.
Abstract
The inhibitory compound of monoamine oxidase (MAO) activity was isolated from the CH(2)Cl(2) fraction of the fructus of Evodia rutaecarpa and identified as 1-methyl-2-undecyl-4(1H)-quinolone (1). Compound 1 showed a selective inhibition of type B MAO (MAO-B) activity with the IC(50) value of 15.3 microM using a substrate kynuramine, but did not inhibit type A MAO (MAO-A) activity. The kinetic analysis using Lineweaver-Burk plots indicated that compound 1 competitively inhibited MAO-B activity with the K(i) value of 9.91 microM. The inhibition of MAO-B by compound 1 was found to be irreversible by dialysis of the incubation mixture. These results suggest that compound 1 is a potent irreversible inhibitor of MAO-B, and may regulate catecholamine content in the neurons.Entities:
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Year: 2003 PMID： 12672993 DOI： 10.1248/cpb.51.409
Source DB: PubMed Journal: Chem Pharm Bull (Tokyo) ISSN： 0009-2363 Impact factor: 1.645