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Literature summary for 1.17.4.1 extracted from

  • Thelander, L.
    Physicochemical characterization of ribonucleoside diphosphate reductase from Escherichia coli (1973), J. Biol. Chem., 248, 4591-4601.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Synthetic peptides which specifically inhibit the activity of virus-induced enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Iron
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
78000
-
alpha,alphabeta2, 2 * 82000 + 2 * 78000, each subunit composed of 2 polypeptide chains, subunit B1, 82000 Da, sedimentation equilibrium centrifugation, subunit B2, low speed sedimentation equilibrium centrifugation Escherichia coli
82000
-
alpha,alphabeta2, 2 * 82000 + 2 * 78000, each subunit composed of 2 polypeptide chains, subunit B1, 82000 Da, sedimentation equilibrium centrifugation, subunit B2, low speed sedimentation equilibrium centrifugation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer alpha,alpha'beta2, 2 * 82000 + 2 * 78000, each subunit composed of 2 polypeptide chains, subunit B1, 82000 Da, sedimentation equilibrium centrifugation, subunit B2, low speed sedimentation equilibrium centrifugation Escherichia coli