
Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase
Author(s) -
Rajib Sengupta,
Arne Holmgren
Publication year - 2014
Publication title -
world journal of biological chemistry
Language(s) - English
Resource type - Journals
ISSN - 1949-8454
DOI - 10.4331/wjbc.v5.i1.68
Subject(s) - ribonucleotide reductase , glutaredoxin , deoxyribonucleotides , thioredoxin , thioredoxin reductase , ribonucleotide , biochemistry , reductase , enzyme , limiting , dna , chemistry , nucleotide , mechanical engineering , protein subunit , engineering , gene
Ribonucleotide reductase (RNR), the rate-limiting enzyme in DNA synthesis, catalyzes reduction of the different ribonucleotides to their corresponding deoxyribonucleotides. The crucial role of RNR in DNA synthesis has made it an important target for the development of antiviral and anticancer drugs. Taking account of the recent developments in this field of research, this review focuses on the role of thioredoxin and glutaredoxin systems in the redox reactions of the RNR catalysis.