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Antioxidant and redox enzymes represent a broad and diverse class of proteins essential for maintaining cellular redox homeostasis by neutralizing reactive oxygen species (ROS) and reactive nitrogen species (RNS). Key members of this group include superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and the thioredoxin/peroxiredoxin systems, which collectively protect cellular components such as DNA, lipids, and proteins from oxidative damage (NIH, 2023; IntechOpen, 2023). These enzymes are critical in the pathogenesis of various conditions, including neurodegenerative diseases, cardiovascular disorders, and cancer, where their dysregulation can lead to chronic inflammation or cell death (MDPI, 2024; BMB Reports, 2015). Therapeutic interventions often focus on enhancing this system through Nrf2 activators like bardoxolone methyl or providing exogenous mimetics such as ebselen to restore balance in high-stress environments (NIH, 2025). Conversely, in oncology, inhibiting these enzymes is explored as a strategy to sensitize tumor cells to pro-oxidant therapies by overwhelming their protective capacity (MDPI, 2020). Monitoring the activity of these enzymes and the levels of oxidative damage products, such as malondialdehyde, serves as a vital biomarker for assessing disease progression and therapeutic efficacy (NIH, 2025).
Drugs targeting this system typically act by activating the Nrf2-Keap1 signaling pathway to induce the expression of endogenous enzymes, providing synthetic mimetics that replicate the catalytic activity of enzymes like SOD or GPx, or inhibiting specific enzymes to increase ROS levels for therapeutic benefit in cancer (NIH, 2023; MDPI, 2024).
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