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Mycobacterial Epoxide Hydrolase EphD Is Inhibited by Urea and Thiourea Derivatives. | LitMetric

Mycobacterial Epoxide Hydrolase EphD Is Inhibited by Urea and Thiourea Derivatives.

Int J Mol Sci

Department of Biochemistry, Faculty of Natural Sciences, Comenius University in Bratislava, Mlynská Dolina, Ilkovičova 6, 842 15 Bratislava, Slovakia.

Published: March 2021

AI Article Synopsis

  • The human pathogen's genome has a high number of epoxide hydrolases involved in lipid metabolism and detoxification, which help it survive in hostile conditions within macrophages.
  • This study investigates the impact of isoxyl, a thiourea drug, on six different epoxide hydrolases using fatty acid substrates.
  • Results indicate that isoxyl significantly inhibits EphD, an enzyme crucial for mycolic acid metabolism in mycobacteria, as shown by changes in mycolic acid profiles and activity in the cells.

Article Abstract

The genome of the human intracellular pathogen encodes an unusually large number of epoxide hydrolases, which are thought to be involved in lipid metabolism and detoxification reactions needed to endure the hostile environment of host macrophages. These enzymes therefore represent suitable targets for compounds such as urea derivatives, which are known inhibitors of soluble epoxide hydrolases. In this work, we studied in vitro the effect of the thiourea drug isoxyl on six epoxide hydrolases of using a fatty acid substrate. We show that one of the proteins inhibited by isoxyl is EphD, an enzyme involved in the metabolism of mycolic acids, key components of the mycobacterial cell wall. By analyzing mycolic acid profiles, we demonstrate the inhibition of EphD epoxide hydrolase activity by isoxyl and two other urea-based inhibitors, thiacetazone and AU1235, inside the mycobacterial cell.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7998700PMC
http://dx.doi.org/10.3390/ijms22062884DOI Listing

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