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揭开过氧化物酶体增殖物激活受体的过氧化物酶活性:对机制、功能和生物学意义的全面综述

Unraveling the Peroxidase Activity in Peroxiredoxins: A Comprehensive Review of Mechanisms, Functions, and Biological Significance.

作者信息

Qausain Sana, Basheeruddin Mohd

机构信息

Biomedical Sciences, Allied Health Sciences, Datta Meghe Institute of Higher Education and Research, Wardha, IND.

Biochemistry, Jawaharlal Nehru Medical College, Datta Meghe Institute of Higher Education and Research, Wardha, IND.

出版信息

Cureus. 2024 Aug 4;16(8):e66117. doi: 10.7759/cureus.66117. eCollection 2024 Aug.

DOI:10.7759/cureus.66117
PMID:39229430
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11370188/
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.

摘要

过氧化物酶体增殖物激活受体(Prxs)是生命三域中每个生物体内必需的抗氧化酶成员,在控制细胞内过氧化物水平方面发挥着关键作用。这篇全面的文献综述旨在阐明Prxs的过氧化物酶活性,研究它们在不同分类群生物体中的作用和意义。具有讽刺意味的是,Prxs的主要作用是过氧化物酶活性,包括还原过氧化氢和其他有机氢过氧化物,并降低细胞内氧化损伤的风险。上述酶活性是通过活性位点中的半胱氨酸残基催化的可逆氧化还原反应形成亚磺酸,并由细胞内还原剂进行还原而发生的。在结构和功能上,Prxs以二聚体或十聚体形式发挥作用,并根据其亚家族或细胞区室表现出不同的催化模式。与Prxs的其他两个亚组(包括2 - 半胱氨酸Prxs和非典型Prxs)的机制相比,1 - 半胱氨酸Prxs具有单体 - 二聚体开关折叠并伴有催化活性。除了广为人知的过氧化物酶活性外,Prxs还被认为参与其他信号传导过程,包括氧化还原信号传导和细胞凋亡。这种对氧化应激的规避以及细胞氧化还原状态的调节使它们成为细胞对环境变化或疾病表现进行适应性反应的核心。总之,基于所获得的数据以及对Prxs结构和功能的进一步了解,这些酶可被归类为一个多样但必不可少的蛋白质家族,它们可以通过过氧化物酶活性有效保护细胞免受氧化应激的不利影响。这表明了二级相互作用,概括为过氧化物解毒或调节信号传导,并确定了它们在多种生物途径中的适用性。这些知识对于增强对基本细胞功能的总体理解以及揭示针对由活性氧产生增加引起的疾病的进一步治疗方法具有重要价值。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/54808d49adc7/cureus-0016-00000066117-i06.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/147a3a7a4988/cureus-0016-00000066117-i01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/2ae6133e6b54/cureus-0016-00000066117-i02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/03c8ebc35ee3/cureus-0016-00000066117-i03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/0c72b6da0bb5/cureus-0016-00000066117-i04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/52d2b96caf8f/cureus-0016-00000066117-i05.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/54808d49adc7/cureus-0016-00000066117-i06.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/147a3a7a4988/cureus-0016-00000066117-i01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/2ae6133e6b54/cureus-0016-00000066117-i02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/03c8ebc35ee3/cureus-0016-00000066117-i03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/0c72b6da0bb5/cureus-0016-00000066117-i04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/52d2b96caf8f/cureus-0016-00000066117-i05.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/36af/11370188/54808d49adc7/cureus-0016-00000066117-i06.jpg

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