Korkmaz, Isil NihanGuller, PinarKalin, RamazanOzdemir, Hasan2026-03-262026-03-2620242365-654910.1002/slct.2024013622-s2.0-85197900582https://doi.org/10.1002/slct.202401362https://hdl.handle.net/20.500.14901/3392GSTs catalyze detoxification reactions of harmful xenobiotics via conjugation with glutathione (GSH) while glutathione reductase (GR) is the sole enzyme that acts in the recovery reaction of GSH from oxidized glutathione (GSSG). In this study, in vitro inhibitory impacts of 3-amino-benzoic acid methyl ester compounds on GR and GST were investigated. For this firstly, GR and GST were obtained from human blood with specific activity of 6.26 EU/mg protein and 8.57 EU/mg protein respectively. Then, inhibition studies were performed. It was found that methyl 3-amino-5-chlorobenzoate had the highest inhibitory effect on hGR with Ki value of 0.524 +/- 0.109 mu M) and methyl 3-amino-4-nitrobenzoate was the most effective inhibitor on hGST with Ki value of 37.05 +/- 4.487 mu M. Besides, molecular docking analysis was used to estimate the binding energies of molecules. Methyl 3-amino-4-nitrobenzoate and methyl 3-amino-4-chlorobenzoate were predicted to have the highest binding affinity into GR and GST receptors respectively.eninfo:eu-repo/semantics/closedAccessGlutathione ReductaseGlutathione S-TransferasesIn Vitro InhibitionMethyl 3-Amino BenzoatesMolecular DockingArticle