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Literature summary for 1.17.4.1 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
Search for more literature for 1.17.4.1

Cloned(Commentary)

Cloned (Comment) Organism
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

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.024
-
 subunit Y1, expressed in Saccharomyces cerevisiae Saccharomyces cerevisiae
0.3
-
 His-tagged subunit Y2-K387N, expressed in Saccharomyces cerevisiae Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Subunits

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