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Literature summary for 1.17.4.1 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

Protein Variants Comment Organism
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
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
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
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

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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