AI Article Synopsis

  • Peroxiredoxins (Prxs) are vital antioxidant enzymes found in all domains of life, playing a key role in reducing hydrogen peroxide and protecting cells from oxidative damage.
  • Their peroxidase activity involves reversible oxidation-reduction processes, primarily facilitated by cysteine residues, and they exist as dimers or decamers, exhibiting different catalytic behaviors based on their specific subfamilies.
  • Beyond their antioxidant roles, Prxs are increasingly recognized for their involvement in signaling pathways, including redox signaling and apoptosis, highlighting their significance in cellular responses to environmental changes and diseases.

Article Abstract

Peroxiredoxins (Prxs) are members of the antioxidant enzymes necessary for every living object in the three domains of life and play critical roles in controlling peroxide levels in cells. This comprehensive literature review aims to elucidate the peroxidase activity of Prxs, examining their roles and significance for organisms across various taxa. Ironically, the primary role of the Prxs is the peroxidase activity, which comprises the reduction of hydrogen peroxide and other organic hydroperoxides and decreases the risk of oxidative damage in the cells. The above enzymatic activity occurs through the reversible oxidation-reduction catalyzed by cysteine residues in the active site by forming sulfenic acid and reduction by intracellular reductants. Structurally and functionally, Prxs function as dimers or decamers and show different catalytic patterns according to their subfamilies or cellular compartments. Compared to the mechanisms of the other two subgroups of Prxs, including 2-Cys Prxs and atypical Prxs, the 1-Cys Prxs have monomer-dimer switch folding coupled with catalytic activity. In addition to their peroxidase activity, which is widely known, Prxs are becoming acknowledged to be involved in other signaling processes, including redox signaling and apoptosis. This aversion to oxidative stress and regulation by the cellular redox state places them at the heart of adaptive cellular responses to changes in the environment or manifestations of diseases. In conclusion, based on the data obtained and on furthering the knowledge of Prxs' structure and function, these enzymes may be classified as a diverse yet essential family of proteins that can effectively protect cells from the adverse effects of oxidative stress due to peroxidase activity. This indicates secondary interactions, summarized as peroxide detoxification or regulatory signaling, and identifies their applicability in multiple biological pathways. Such knowledge is valuable for enhancing the general comprehension of essential cellular functions and disclosing further therapeutic approaches to the diseases caused by the increased production of reactive oxygen species.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11370188PMC
http://dx.doi.org/10.7759/cureus.66117DOI Listing

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