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Literature summary for 1.17.4.1 extracted from

  • Vitols, E.; Bauer, V.A.; Stanbrough, E.C.
    Ribonucleotide reductase from Saccharomyces cerevisiae (1970), Biochem. Biophys. Res. Commun., 41, 71-77.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
phosphate 50 mM, slight stimulation, inhibition at 200 mM Saccharomyces cerevisiae

General Stability

General Stability Organism
partially purified enzyme is very unstable in solution, half-life at 0°C: less than 24 h Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
additional information
-
Herpes simplex virus
additional information not inhibited by 8-hydroxyquinoline and o-phenanthroline Saccharomyces cerevisiae
YAGAVVNDL peptide may prevent association of the two subunits by competing for the subunit binding site Herpes simplex virus
YGAVVNDL
-
Herpes simplex virus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
thioredoxin
-
Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Herpes simplex virus
-
type 1, HSV-1
-
Saccharomyces cerevisiae
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0072
-
-
Saccharomyces cerevisiae

Storage Stability

Storage Stability Organism
quick-freezing in liquid nitrogen and subsequent storage at -20°C, several weeks, no loss of activity Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ribonucleoside diphosphate + reduced thioredoxin
-
Herpes simplex virus 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
ir
ribonucleoside diphosphate + reduced thioredoxin maximal activity with E. coli thioredoxin Saccharomyces cerevisiae 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
ir