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Literature summary for 1.17.4.1 extracted from
- Enzymatically active mammalian ribonucleotide reductase exists primarily as an alpha6beta2 octamer (2006), J. Biol. Chem., 281, 27705-27711.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| dATP | 0.05 mM, 10% residual activity | Mus musculus |  |
| dGTP | 0.1 mM, 12% residual activity | Mus musculus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | in presence of dTTP, subunit R1 forms dimers. In presence of dATP or ATP, subunit R1 forms hexamers of 544000 Da, which interact with the subunit R2 dimer to form an enzymatically active protein complex alpha6beta2. The complex can be in activated or inhibited state depending on whether ATP or dATP is bound. Complex alpha6beta2 is the major form of enzyme at physiological levels of subunits and nucleotides | Mus musculus |
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