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Inhibition of Monoamine Oxidase by Anithiactins from Streptomyces sp.

Title
Inhibition of Monoamine Oxidase by Anithiactins from Streptomyces sp.
Authors
Lee, Hyun WooJung, Won KyeongKim, Hee JungJeong, Yu SeokNam, Sang-JipKang, HeonjoongKim, Hoon
Ewha Authors
남상집
SCOPUS Author ID
남상집scopus
Issue Date
2015
Journal Title
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
ISSN
1017-7825JCR Link1738-8872JCR Link
Citation
vol. 25, no. 9, pp. 1425 - 1428
Keywords
Anithiactin Amonoamine oxidaseStreptomyces sp.selective inhibitorcompetitive inhibitor
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Indexed
SCIE; SCOPUS; KCI WOS scopus
Abstract
Monoamine oxidase (MAO) is found in most cell types and catalyzes the oxidation of monoamines. Three anithiactins (A-C, modified 2-phenylthiazoles) isolated from Streptomyces sp. were tested for inhibitory activity of two isoforms, MAO-A and MAO-B. Anithiactin A was effective and selective for the inhibition of MAO-A, with an IC50 value of 13.0 mu M; however, it was not effective for the inhibition of MAO-B. Anithiactins B and C were weaker inhibitors for MAO-A and MAO-B. Anithiactin A was a reversible and competitive inhibitor for MAO-A with a K-i value of 1.84 mu M. The hydrophobic methyl substituent in anithiactin A may play an important role in the inhibition of MAO-A. It is suggested that anithiactin A is a selective reversible inhibitor for MAO-A, with moderate potency, and can be considered a new potential lead compound for further development of novel reversible inhibitors for MAO-A.
DOI
10.4014/jmb.1505.05020
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자연과학대학 > 화학·나노과학전공 > Journal papers
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