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Mycobacterial Epoxide Hydrolase EphD Is Inhibited by Urea and Thiourea Derivatives.
Int J Mol Sci
March 2021
Department of Biochemistry, Faculty of Natural Sciences, Comenius University in Bratislava, Mlynská Dolina, Ilkovičova 6, 842 15 Bratislava, Slovakia.
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.
View Article and Find Full Text PDFNew insights into the chemical behavior of S-oxide derivatives of thiocarbonyl-containing antitubercular drugs and the influence on their mechanisms of action and toxicity.
Ann Pharm Fr
March 2019
CNRS, Laboratoire de Chimie de Coordination, LCC, UPR 8241, 205, route de Narbonne, BP 44099, 31077 Toulouse, cedex 4, France. Electronic address:
Objectives: This work aims at getting more insights into the distinct behavior of S-oxide derivatives of thiocarbonyl-containing antitubercular drugs, in order to better understand their mechanism of action and toxicity.
Methods: Computational calculation of relative free energy (ΔΔG) of S-oxide tautomers (sulfine R-C [SO]NH2), sulfenic acid (R-C [S-OH]NH) and sulfoxide (R-C [SHO]NH) derived from thioamide and thiourea antitubercular drugs and an update of the literature data with a new point of view about how the structural features of oxidized primary metabolites (S-oxide) can influence the outcome of the reactions and be determinant for the mechanisms of action and of toxicity of these drugs.
Results: The calculated free energy of S-oxide tautomers, derived from thioamide and thiourea-type antitubercular drugs, supported by some experimental results, revealed that S-oxide derivatives could be found under sulfine and sulfenic acid forms depending on their chemical structures.
Repositioning of Thiourea-Containing Drugs as Tyrosinase Inhibitors.
Int J Mol Sci
December 2015
Research Institute of Pharmaceutical Sciences, College of Pharmacy, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 702-701, Korea.
Tyrosinase catalyzes two distinct sequential reactions in melanin biosynthesis: The hydroxylation of tyrosine to dihydroxyphenylalanine (DOPA) and the oxidation of DOPA to dopaquinone. Developing functional modulators of tyrosinase is important for therapeutic and cosmetic purposes. Given the abundance of thiourea moiety in known tyrosinase inhibitors, we studied other thiourea-containing drugs as potential tyrosinase inhibitors.
View Article and Find Full Text PDFInhibitory Potential of Twenty Five Anti-tuberculosis Drugs on CYP Activities in Human Liver Microsomes.
Biol Pharm Bull
June 2016
Department of Drug Metabolism, Tokushima Research Institute, Otsuka Pharmaceutical Co., Ltd.
The direct inhibitory potential of twenty five anti-tuberculosis drugs on eight CYP-specific reactions in human liver microsomes was investigated to predict in vivo drug-drug interactions (DDIs) from in vitro data. Rifampicin, rifabutin, and thioacetazone inhibited one CYP reaction. Isoniazid and clofazimine had inhibitory effects on four CYP reactions, and rifapentine, ethionamide, and prothionamide widely inhibited CYP reactions.
View Article and Find Full Text PDFPharmacovigilance and tuberculosis: applying the lessons of thioacetazone.
Bull World Health Organ
December 2014
Global TB Programme, World Health Organization, avenue Appia 20, 1211 Geneva 27, Switzerland .
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