Xanthine oxidoreductase: structure, distribution and physioloical role

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Аннотация

The article presents an overview of the modern literature on the structure, distribution, biological and physiological role of xanthine oxidoreductase (XOR). XOR has been identified in all living organisms, from bacteria to humans. However, only in mammals it is presented in two forms, other species contain exclusively the XDH form. The enzyme is a homodimer with independent electron transfer in each monomer. XOR catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid in the final stage of purine metabolism and is widely distributed enzyme. The review highlights the forms of XOR and their role in the generation of reactive oxygen species (ROS), reactive nitrogen species (RNS) and synthesis of uric acid which are involved in many physiological processes. Uric acid shows antioxidant activity, and ROS and RNS play a role in innate immunity, in signaling, metabolism of xenobiotics, regulation of cellular redox potential and are also involved in mammogenesis and lactogenesis. Thus, in recent years significant progress has been made in understanding the biochemical and physiological nature of this enzyme system.

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Авторлар туралы

S. Bedina

Federal State Budgetary Institution “Research Institute of Clinical and Experimental Rheumatology named after A.B. Zborovsky”; Volgograd State Medical University

Хат алмасуға жауапты Автор.
Email: clinicalbiochemistry@yandex.ru
Ресей, 400138, Volgograd; 400131, Volgograd

E. Mozgovaya

Federal State Budgetary Institution “Research Institute of Clinical and Experimental Rheumatology named after A.B. Zborovsky”

Email: nauka@pebma.org
Ресей, 400138, Volgograd

S. Spitsina

Federal State Budgetary Institution “Research Institute of Clinical and Experimental Rheumatology named after A.B. Zborovsky”; Volgograd State Medical University

Email: svetlanahime@yandex.ru
Ресей, 400138, Volgograd; 400131, Volgograd

M. Mamus

Federal State Budgetary Institution “Research Institute of Clinical and Experimental Rheumatology named after A.B. Zborovsky”

Email: m.mamus@yandex.ru
Ресей, 400138, Volgograd

A. Trofimenko

Federal State Budgetary Institution “Research Institute of Clinical and Experimental Rheumatology named after A.B. Zborovsky”

Email: a.s.trofimenko@mail.ru
Ресей, 400138, Volgograd

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2. Fig. 1. Molecular structure of the xanthine oxidoreductase (XOR) monomer. The XOR monomer includes an N-terminal 2Fe/S domain (molecular weight 20 kDa), an intermediate FAD domain (molecular weight 40 kDa), and a C-terminal Mo-Co domain (molecular weight 85 kDa).

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3. Fig. 2. Scheme of oxidative hydroxylation of hypoxanthine and xanthine to uric acid with the formation of active oxygen species.

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4. Fig. 3. Biological functions of KOR and products of the reaction catalyzed by the enzyme.

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5. Fig. 4. Functional capabilities of the KOR in various organs.

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