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Literature summary extracted from

  • Kashlan, O.B.; Scott, C.P.; Lear, J.D.; Cooperman, B.S.
    A comprehensive model for the allosteric regulation of mammalian ribonucleotide reductase. Functional consequences of ATP- and dATP-induced oligomerization of the large subunit (2002), Biochemistry, 41, 462-474.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.17.4.1 dATP 0.2-0.4 mM, induces formation of dimers and tetramers of subunit R1, 1-2 mM, induces formation of hexamers of subunit R1 Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.1 Mus musculus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.1 ribonucleoside diphosphate + reduced thioredoxin CDP is the only substrate that is reduced with a significant activity even in the absence of allosteric effectors Mus musculus 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.17.4.1 More nucleotide binding to the specificity site drives formation of an active R1,2R2,2 dimer, ATP or dATP binding to the adenine-specific site results in formation of an inactive tetramer and ATP binding to the hexamerization site drives formation of an active R1,6R2,6 hexamer which is probably the major active form in mammalian cells Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.17.4.1 0.047
-
 CDP CDP reduction in the absence of allosteric effectors Mus musculus
1.17.4.1 0.16
-
 CDP CDP reduction in the presence of 1 mM ATP Mus musculus
1.17.4.1 0.26
-
 CDP CDP reduction in the presence of 0.2 mM ATP Mus musculus
1.17.4.1 0.29
-
 CDP CDP reduction in the presence of 4 mM ATP Mus musculus