Biochemical properties of Glutathione S-transferase, as a potential target for cancer chemotherapy | ||
| Bulletin of Faculty of Science, Zagazig University | ||
| Article 21, Volume 2025, Issue 3, July 2025, Pages 230-235 PDF (610.77 K) | ||
| Document Type: Original Article | ||
| DOI: 10.21608/bfszu.2025.357880.1476 | ||
| Author | ||
| Ashraf Elsayed* | ||
| Abstract | ||
| Glutathione S-transferase is a one of the most remarkable phase II detoxifying enzymes, via catalyzing the conjugation of reduced glutathione to numerous intrinsic and extrinsic xenobiotic or toxic compounds. Glutathione S-transferases are dimeric enzymes, with each monomer containing two distinct domains, the N-terminal domain is the frequently conserved one, because it includes the central moieties of the active site, called the glutathione binding area, the G-site. The GST catalyze the conjugation of the different xenobiotic compounds “herbicides and pesticides” with the electrophilic center to glutathione. Epothilone B appeared more active than Taxol in the tubulin polymerization; it replaced Taxol that bounded to microtubules. Epothilone has a higher activity than Paclitaxel against P-glycoprotein-expressing multiple-drug-resistant cell lines. This review has been focused to give an insight about the biochemical and molecular properties of fungal GST, as well as, the possibility of construction of a new derivative of Epothilone via conjugation with reduced glutathione. | ||
| Keywords | ||
| Glutathione S-Transferase; Epothilone; Fungi; detoxifying enzyme | ||
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