Glutathione S-transferase (GST) is one of the most remarkable phase II detoxifying enzymes, catalyzing the conjugation of reduced glutathione to numerous intrinsic and extrinsic xenobiotic or toxic compounds. GSTs are dimeric enzymes, with each monomer containing two distinct domains. The N-terminal domain is the most conserved, as it contains the glutathione binding area (G-site). GST catalyzes the conjugation of various xenobiotic compounds, such as herbicides and pesticides, with glutathione at their electrophilic centers. Epothilone B has shown higher activity than Taxol in tubulin polymerization, replacing Taxol at the microtubule-binding site, and demonstrates greater activity than Paclitaxel against P-glycoprotein-expressing multidrug-resistant cell lines. This review provides an insight into the biochemical and molecular properties of fungal GSTs and explores the possibility of constructing a novel epothilone derivative via conjugation with reduced glutathione