|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 188.8.131.52
Mass balance status: Balanced.
Enzyme Commission Primary Name: ribonucleoside-diphosphate reductase
Enzyme Commission Synonyms: 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
This reaction synthesizes deoxynucleoside diphosphates. Thioredoxin is the reductant cofactor and NADPH is the ultimate hydrogen donor.
Enzyme Commission Summary:
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 [Larsson66, Qiu06].
Larsson66: Larsson A, Reichard P (1966). "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(11);2533-9. PMID: 5330119
Larsson66a: Larsson A, Reichard P (1966). "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(11);2540-9. PMID: 5330120
Larsson73: Larsson A (1973). "Ribonucleotide reductase from regenerating rat liver. II. Substrate phosphorylation level and effect of deoxyadenosine triphosphate." Biochim Biophys Acta 324(4);447-51. PMID: 4543472
Qiu06: Qiu W, Zhou B, Darwish D, Shao J, Yen Y (2006). "Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits." Biochem Biophys Res Commun 340(2);428-34. PMID: 16376858
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493