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Literature summary extracted from

  • Narvaez, A.J.; Voevodskaya, N.; Thelander, L.; Graeslund, A.
    The involvement of Arg265 of mouse ribonucleotide reductase R2 protein in proton transfer and catalysis (2006), J. Biol. Chem., 281, 26022-26028.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.17.4.1 R265A mutant in subunit R2, about 10% of wild-type activity. Mutant is able to form stable tyrosyl radicals and bind subunit R1 with similar kinetics as wild-type Mus musculus
1.17.4.1 R265E mutant in subunit R2, about 40% of wild-type activity. Mutant is able to form stable tyrosyl radicals and bind subunit R1 with similar kinetics as wild-type Mus musculus
1.17.4.1 R265Q mutant in subunit R2, about 1% of wild-type activity. Mutant is able to form stable tyrosyl radicals and bind subunit R1 with similar kinetics as wild-type Mus musculus
1.17.4.1 R265Y mutant in subunit R2, about 4% of wild-type activity. Mutant is able to form stable tyrosyl radicals and bind subunit R1 with similar kinetics as wild-type Mus musculus

Organism

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.17.4.1 116
-
 mutant R265Y, pH 7.5, 37°C Mus musculus
1.17.4.1 283
-
 mutant R265A, pH 7.5, 37°C Mus musculus
1.17.4.1 1100
-
 mutant R265E, pH 7.5, 37°C Mus musculus
1.17.4.1 2750
-
 wild-type, pH 7.5, 37°C Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.1 CDP + reduced dithiothreitol
-
 Mus musculus 2'-dCDP + oxidized dithiothreitol + H2O
-
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