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Literature summary for 1.17.4.1 extracted from

  • Bunker, G.; Petersson, L.; Sjöberg, B.M.; Sahlin, M.; Chance, M.; Chance, B.; Ehrenberg, A.
    Extended X-ray absorption fine structure studies on the iron-containing subunit of ribonucleotide reductase from Escherichia coli (1987), Biochemistry, 26, 4708-4716.
    View publication on PubMed
Search for more literature for 1.17.4.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Iron X-ray absorption fine structure, EXAFS, of iron-containing subunit, Fe-Fe distance in subunit B2 is in the 3.26-3.48 A range Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
chimeric R2 genes in which C-terminal sequences in Escherichia coli subunit R2 are replaced by C-terminal sequences from the mouse subunit R2 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3
-
 recombinant B2 subunit 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