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探索哺乳动物血红素过氧化物酶:髓过氧化物酶、乳过氧化物酶、嗜酸性粒细胞过氧化物酶、甲状腺过氧化物酶和过氧化物酶的结构和功能的综合评述。

Exploring mammalian heme peroxidases: A comprehensive review on the structure and function of myeloperoxidase, lactoperoxidase, eosinophil peroxidase, thyroid peroxidase and peroxidasin.

机构信息

Department of Biotechnology, Sharda School of Engineering and Technology, Sharda University, P.C. 201310, Greater Noida, U.P., India.

School of Biotechnology, Gautam Buddha University, P.C. 201312, Greater Noida, U.P., India.

出版信息

Arch Biochem Biophys. 2024 Nov;761:110155. doi: 10.1016/j.abb.2024.110155. Epub 2024 Sep 13.

DOI:10.1016/j.abb.2024.110155
PMID:39278306
Abstract

The peroxidase family of enzymes is a ubiquitous cluster of enzymes primarily responsible for the oxidation of organic and inorganic substrates. The mammalian heme peroxidase subfamily is characterized by a covalently linked heme prosthetic group which plays a key role in the oxidation of halides and psuedohalides into their respective hypohalous acid and hypothiocyanous acid under the influence of HO as substrate. The members of the heme peroxidase family include Lactoperoxidase (LPO), Eosinophil peroxidase (EPO), Myeloperoxidase (MPO), Thyroid peroxidase (TPO) and Peroxidasin (PXDN). The biological activity of LPO, MPO and EPO pertains to antibacterial, antifungal and antiviral while TPO is involved in the biosynthesis of the thyroid hormone and PXDN helps maintain the ECM. While these enzymes play several immunomodulatory roles, aberrations in their activity have been implicated in diseases such as myocardial infarction, asthma and Alzheimer's amongst others. The sequence and structural similarities amongst the members of the family are strikingly high while the substrate specificities and subcellular locations vary. Hence, it becomes important to provide a consortium of information regarding the members to study their biochemical, pathological and clinical function.

摘要

过氧化物酶家族的酶是一类普遍存在的酶簇,主要负责有机和无机底物的氧化。哺乳动物血红素过氧化物酶亚家族的特征是与血红素辅基共价连接,血红素辅基在 HO 作为底物的影响下,在卤化物和拟卤化物氧化为相应的次卤酸和次硫氰酸中起着关键作用。过氧化物酶家族的成员包括乳过氧化物酶 (LPO)、嗜酸性粒细胞过氧化物酶 (EPO)、髓过氧化物酶 (MPO)、甲状腺过氧化物酶 (TPO) 和过氧化物酶体 (PXDN)。LPO、MPO 和 EPO 的生物学活性与抗菌、抗真菌和抗病毒有关,而 TPO 参与甲状腺激素的生物合成,PXDN 有助于维持 ECM。虽然这些酶发挥了几种免疫调节作用,但它们活性的异常与心肌梗死、哮喘和阿尔茨海默病等疾病有关。该家族成员之间的序列和结构相似性非常高,而底物特异性和亚细胞位置则有所不同。因此,提供有关该家族成员的信息联合体对于研究它们的生化、病理和临床功能变得非常重要。

相似文献

1
Exploring mammalian heme peroxidases: A comprehensive review on the structure and function of myeloperoxidase, lactoperoxidase, eosinophil peroxidase, thyroid peroxidase and peroxidasin.探索哺乳动物血红素过氧化物酶:髓过氧化物酶、乳过氧化物酶、嗜酸性粒细胞过氧化物酶、甲状腺过氧化物酶和过氧化物酶的结构和功能的综合评述。
Arch Biochem Biophys. 2024 Nov;761:110155. doi: 10.1016/j.abb.2024.110155. Epub 2024 Sep 13.
2
Peroxidasin and eosinophil peroxidase, but not myeloperoxidase, contribute to renal fibrosis in the murine unilateral ureteral obstruction model.过氧化物酶和嗜酸性粒细胞过氧化物酶,但不是髓过氧化物酶,有助于在单侧输尿管梗阻模型的小鼠肾脏纤维化。
Am J Physiol Renal Physiol. 2019 Feb 1;316(2):F360-F371. doi: 10.1152/ajprenal.00291.2018. Epub 2018 Dec 19.
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Biosynthesis of human myeloperoxidase.人髓过氧化物酶的生物合成。
Arch Biochem Biophys. 2018 Mar 15;642:1-9. doi: 10.1016/j.abb.2018.02.001. Epub 2018 Feb 3.
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Kinetics of interconversion of redox intermediates of lactoperoxidase, eosinophil peroxidase and myeloperoxidase.乳过氧化物酶、嗜酸性粒细胞过氧化物酶和髓过氧化物酶氧化还原中间体的相互转化动力学
Jpn J Infect Dis. 2004 Oct;57(5):S30-1.
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Redox thermodynamics of lactoperoxidase and eosinophil peroxidase.乳过氧化物酶和嗜酸性粒细胞过氧化物酶的氧化还原热力学。
Arch Biochem Biophys. 2010 Feb 1;494(1):72-7. doi: 10.1016/j.abb.2009.11.021. Epub 2009 Nov 26.
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Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control.人血红素蛋白的过氧化物酶活性:控制火势。
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How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase.共价血红素与蛋白质的键如何影响一种细菌过氧化物酶的氧化还原中间体的形成和反应性。
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Structural basis of activation of mammalian heme peroxidases.哺乳动物血红素过氧化物酶激活的结构基础。
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Thiocyanate modulates the catalytic activity of mammalian peroxidases.硫氰酸盐可调节哺乳动物过氧化物酶的催化活性。
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Halogenation Activity of Mammalian Heme Peroxidases.哺乳动物血红素过氧化物酶的卤化活性。
Antioxidants (Basel). 2022 Apr 30;11(5):890. doi: 10.3390/antiox11050890.

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