Akademik Veri Yönetim Sistemi
Spectroscopy Letters, 2026 (SCI-Expanded, Scopus)
The enzyme glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49) is the first and rate-limiting enzyme of the pentose phosphate pathway, which is essential for the integrity and function of red blood cells. NADPH, produced in this metabolic pathway, acts as a protector of anabolic pathways in the liver and plays a crucial role in energy metabolism. In this study, G6PD was purified 6308-fold in a single step by affinity chromatography from sheep liver. The molecular weight of the G6PD enzyme was found to be 93 kDa with SDS-PAGE. The Vmax and KM values for the G6P substrate were calculated as 0.58 EU/mL (47.94 EU/mg protein) and 1.44 mM, respectively. The effect of biotin (vitamin B7) and folic acid (vitamin B9) on G6PD activity was examined. Biotin and folic acid had a significantly inhibitory effect on G6PD activity. The IC50 values of biotin and folic acid vitamins were calculated as 61.64 µM and 17.21 µM, respectively. Ki values and inhibition type were determined using Lineweaver-Burk plots. The inhibitory type of these vitamins was determined to be noncompetitive. Ki values for biotin and folic acid were calculated as 121.13 µM and 22.73 µM, respectively. The increased activity of the G6PD enzyme in various cancer diseases facilitates the rapid development of cancer cells. Therefore, G6PD inhibitors can be a very important treatment method in cancer treatment. Here, the fact that biotin and folic acid vitamins exhibit a significant in vitro inhibitory effect on the G6PD enzyme, as well as being naturally occurring, is of further importance.