Inhibition of monoamine oxidase by anithiactins from Streptomyces sp
- 주제(키워드) Anithiactin A , Competitive inhibitor , Monoamine oxidase , Selective inhibitor , Streptomyces sp
- 등재 SCIE, KCI등재, SCOPUS
- 발행기관 Korean Society for Microbiolog and Biotechnology
- 발행년도 2015
- 총서유형 Journal
- URI http://www.dcollection.net/handler/ewha/000000119526
- 본문언어 영어
- Published As http://dx.doi.org/10.4014/jmb.1505.05020
- 저작권 이화여자대학교 논문은 저작권에 의해 보호받습니다.
초록/요약
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 IC<inf>50</inf> value of 13.0 μM; 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<inf>i</inf> value of 1.84 μM. 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. © 2015 by The Korean Society for Microbiology and Biotechnology.
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