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Literature summary extracted from

  • Nguyen, H.H.T.; Ge, J.; Perlstein, D.L.; Stubbe, J.
    Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly (1999), Proc. Natl. Acad. Sci. USA, 96, 12339-12344.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.17.4.1 expression of subunits Y1, Y2, Y3 and Y4 in Escherichia coli, expression of Y1, His-tagged Y2 and His tagged Y2-K387N mutant enzyme subunit in Saccharomyces cerevisiae Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.17.4.1 K387N affords higher activity due to increased tyrosyl radical content Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.1 Saccharomyces cerevisiae
-
-
-

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 0.024
-
 subunit Y1, expressed in Saccharomyces cerevisiae Saccharomyces cerevisiae
1.17.4.1 0.3
-
 His-tagged subunit Y2-K387N, expressed in Saccharomyces cerevisiae Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.1 ribonucleoside diphosphate + reduced thioredoxin
-
 Saccharomyces cerevisiae 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
 ir

Subunits

EC Number Subunits Comment Organism
1.17.4.1 More subunits Y1 and Y2 constitute the active enzyme, large subunit Y3 has no activity, subunit Y4 may function as a chaperone Saccharomyces cerevisiae