Published online Feb 26, 2014. doi: 10.4331/wjbc.v5.i1.68
Revised: December 17, 2013
Accepted: January 13, 2014
Published online: February 26, 2014
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.
Core tip: Thioredoxin and glutaredoxin-mediated redox regulations of ribonucleotide reductase (RNR) catalysis play a vital role as the RNR catalysis involves different redox active thiol functions, thiyl radicals and thiol proteins. The in depth knowledge of the whole redox catalysis will contribute significantly to designing and developing new RNR inhibitors for improved cancer chemotherapy, antibiotic development and antiviral treatments.