Inhibition of monoamine oxidase by anithiactins from Streptomyces sp

Hyun Woo Lee, Won Kyeong Jung, Hee Jung Kim, Yu Seok Jeong, Sang Jip Nam, Heonjoong Kang, Hoon Kim

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17 Scopus citations


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 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 Ki 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.

Original languageEnglish
Pages (from-to)1425-1428
Number of pages4
JournalJournal of Microbiology and Biotechnology
Issue number9
StatePublished - 2 Jun 2015

Bibliographical note

Publisher Copyright:
© 2015 by The Korean Society for Microbiology and Biotechnology.


  • Anithiactin A
  • Competitive inhibitor
  • Monoamine oxidase
  • Selective inhibitor
  • Streptomyces sp


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