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Literature summary extracted from

  • Sato, A.; Cory, J.G.
    Differential sensitivities of the subunits of mammalian ribonucleotide reductase to proteases, sulfhydryl reagents, and heat (1986), Arch. Biochem. Biophys., 244, 572-579.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.17.4.1 dTTP
-
 Mus musculus

General Stability

EC Number General Stability Organism
1.17.4.1 effector-binding subunit of mammalia is more sensitive to proteolysis by chymotrypsin, to heating at 55°C and to sulfhydryl reagents e.g. p-chloromercuribenzoate and N-ethylmaleimide, than the nonheme iron subunit, the latter is more sensitive to trypsin treatment Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.1 Mus musculus
-
 Ehrlich ascites tumor cells
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.4.1 Ehrlich ascites carcinoma cell
-
 Mus musculus
-
1.17.4.1 L-1210 cell
-
 Mus musculus
-
1.17.4.1 L-cell cell line 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
-
 Mus musculus 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
 ir

Subunits

EC Number Subunits Comment Organism
1.17.4.1 More enzyme in Ehrlich ascites tumor cells consits of two nonidentical subunits: an effector-binding subunit, EB, and a non-heme iron containing subunit, NHI, since their relative levels are not coordinately regulated the stoichiometry of the whole enzyme varies with the cell cycle Mus musculus