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Inhibition of Monoamine Oxidase by Anithiactins from Streptomyces sp.
- Inhibition of Monoamine Oxidase by Anithiactins from Streptomyces sp.
- Lee, Hyun Woo; Jung, Won Kyeong; Kim, Hee Jung; Jeong, Yu Seok; Nam, Sang-Jip; Kang, Heonjoong; Kim, Hoon
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY vol. 25, no. 9, pp. 1425 - 1428
- Anithiactin A; monoamine oxidase; Streptomyces sp.; selective inhibitor; competitive inhibitor
- KOREAN SOC MICROBIOLOGY &
- SCIE; SCOPUS; KCI
- Document Type
- 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.
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