Reaction: 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
Other name(s): ribonucleotide reductase; CDP reductase; ribonucleoside diphosphate reductase; UDP reductase; ADP reductase; nucleoside diphosphate reductase; ribonucleoside 5'-diphosphate reductase; ribonucleotide diphosphate reductase; 2'-deoxyribonucleoside-diphosphate:oxidized-thioredoxin 2'-oxidoreductase; RR
Systematic name: 2'-deoxyribonucleoside-diphosphate:thioredoxin-disulfide 2'-oxidoreductase
Comments: This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. An iron protein. While the enzyme is activated by ATP, it is inhibited by dATP [3,6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9047-64-7
1. Lammers, M. and Follmann, H. The ribonucleotide reductases - a unique group of metalloenzymes essential for cell-proliferation. Struct. Bonding 54 (1983) 27-91.
2. Larsson, A. Ribonucleotide reductase from regenerating rat liver. II. Substrate phosphorylation level and effect of deoxyadenosine triphosphate. Biochim. Biophys. Acta 324 (1973) 447-451. [PMID: 4543472]
3. Larsson, A. and Reichard, P. Enzymatic synthesis of deoxyribonucleotides. IX. Allosteric effects in the reduction of pyrimidine ribonucleotides by the ribonucleoside diphosphate reductase system of Escherichia coli. J. Biol. Chem. 241 (1966) 2533-2539. [PMID: 5330119]
4. Larsson, A. and Reichard, P. Enzymatic synthesis of deoxyribonucleotides. X. Reduction of purine ribonucleotides; allosteric behavior and substrate specificity of the enzyme system from Escherichia coli B. J. Biol. Chem. 241 (1966) 2540-2549. [PMID: 5330120]
5. Moore, E.C. and Hurlbert, R.B. Regulation of mammalian deoxyribonucleotide biosynthesis by nucleotides as activators and inhibitors. J. Biol. Chem. 241 (1966) 4802-4809. [PMID: 5926184]
6. Qiu, W., Zhou, B., Darwish, D., Shao, J. and Yen, Y. Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. Biochem. Biophys. Res. Commun. 340 (2006) 428-434. [PMID: 16376858]