دورية أكاديمية
Ribonucleotide reductase: Implications of thiol S-nitrosylation and tyrosine nitration for different subunits.
| العنوان: | Ribonucleotide reductase: Implications of thiol S-nitrosylation and tyrosine nitration for different subunits. |
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| المؤلفون: | Chakraborty S; Amity Institute of Biotechnology, Amity University, Kolkata, 700135, West Bengal, India., Mukherjee P; Amity Institute of Biotechnology, Amity University, Kolkata, 700135, West Bengal, India., Sengupta R; Amity Institute of Biotechnology, Amity University, Kolkata, 700135, West Bengal, India. Electronic address: rsengupta@kol.amity.edu. |
| المصدر: | Nitric oxide : biology and chemistry [Nitric Oxide] 2022 Oct 01; Vol. 127, pp. 26-43. Date of Electronic Publication: 2022 Jul 15. |
| نوع المنشور: | Journal Article; Review |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 9709307 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1089-8611 (Electronic) Linking ISSN: 10898603 NLM ISO Abbreviation: Nitric Oxide Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: <2000- > : San Diego, CA : Elsevier Original Publication: Orlando, FL : Academic Press, c1997- |
| مواضيع طبية MeSH: | Ribonucleotide Reductases*/genetics , Ribonucleotide Reductases*/metabolism, Catalysis ; Catalytic Domain ; Sulfhydryl Compounds ; Tyrosine |
| مستخلص: | Ribonucleotide reductase (RNR) is a multi-subunit enzyme responsible for catalyzing the rate-limiting step in the production of deoxyribonucleotides essential for DNA synthesis and repair. The active RNR complex is composed of multimeric R1 and R2 subunits. The RNR catalysis involves the formation of tyrosyl radicals in R2 subunits and thiyl radicals in R1 subunits. Despite the quaternary structure and cofactor diversity, all the three classes of RNR have a conserved cysteine residue at the active site which is converted into a thiyl radical that initiates the substrate turnover, suggesting that the catalytic mechanism is somewhat similar for all three classes of the RNR enzyme. Increased RNR activity has been associated with malignant transformation, cancer cell growth, and tumorigenesis. Efforts concerning the understanding of RNR inhibition in designing potent RNR inhibitors/drugs as well as developing novel approaches for antibacterial, antiviral treatments, and cancer therapeutics with improved radiosensitization have been made in clinical research. This review highlights the precise and potent roles of NO in RNR inhibition by targeting both the subunits. Under nitrosative stress, the thiols of the R1 subunits have been found to be modified by S-nitrosylation and the tyrosyl radicals of the R2 subunits have been modified by nitration. In view of the recent advances and progresses in the field of nitrosative modifications and its fundamental role in signaling with implications in health and diseases, the present article focuses on the regulations of RNR activity by S-nitrosylation of thiols (R1 subunits) and nitration of tyrosyl residues (R2 subunits) which will further help in designing new drugs and therapies. (Copyright © 2022 Elsevier Inc. All rights reserved.) |
| المشرفين على المادة: | 0 (Sulfhydryl Compounds) 42HK56048U (Tyrosine) EC 1.17.4.- (Ribonucleotide Reductases) |
| تواريخ الأحداث: | Date Created: 20220719 Date Completed: 20220823 Latest Revision: 20220902 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1016/j.niox.2022.07.002 |
| PMID: | 35850377 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1089-8611 |
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| DOI: | 10.1016/j.niox.2022.07.002 |