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Literature summary extracted from

  • Booker, S.; Licht, S.; Broderick, J.; Stubbe, J.
    Coenzyme B12-dependent ribonucleotide reductase: evidence for the participation of five cysteine residues in ribonucleotide reduction (1994), Biochemistry, 33, 12676-12685.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.17.4.2 cloning, sequencing and expression of the protein Lactobacillus leichmannii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.17.4.2 82000
-
-
 Lactobacillus leichmannii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.4.2 ribonucleoside triphosphate + reduced thioredoxin + H2O Lactobacillus leichmannii
-
 2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.2 Lactobacillus leichmannii
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.2 ribonucleoside triphosphate + reduced thioredoxin
-
 Lactobacillus leichmannii 2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
 r
1.17.4.2 ribonucleoside triphosphate + reduced thioredoxin + H2O
-
 Lactobacillus leichmannii 2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
 r

Subunits

EC Number Subunits Comment Organism
1.17.4.2 monomer
-
 Lactobacillus leichmannii

Synonyms

EC Number Synonyms Comment Organism
1.17.4.2 RTPR
-
 Lactobacillus leichmannii

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.4.2 coenzyme B12 adenosylcobalamin Lactobacillus leichmannii