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Literature summary for 1.17.4.2 extracted from

  • Chen, D.; Abend, A.; Stubbe, J.; Frey, P.A.
    Epimerization at carbon-5' of (5'R)-[5'-2H]adenosylcobalamin by ribonucleoside triphosphate reductase: cysteine 408-independent cleavage of the Co-C5'-bond (2003), Biochemistry, 42, 4578-4584.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dGTP both epimerization and 5'-hydrogen exchange reactions are stimulated by the allosteric effector Lactobacillus leichmannii

Protein Variants

Protein Variants Comment Organism
C408A only wild-type enzyme catalyzes epimerization of the (5'S)-[5'-2H1]- and (5'R)-[5'-2H1]-isotopomers of adenosylcobalamin, no activity of mutant enzyme Lactobacillus leichmannii
C408S only wild-type enzyme catalyzes epimerization of the (5'S)-[5'-2H1]- and (5'R)-[5'-2H1]-isotopomers of adenosylcobalamin, no activity of mutant enzyme Lactobacillus leichmannii

Organism

Organism UniProt Comment Textmining
Lactobacillus leichmannii
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme also catalyzes the exchange of the C5'-hydrogens of adenosylcobalamin with solvent hydrogen, epimerization of the (5'S)-[5'-2H1]- and (5'R)-[5'-2H1]-isotopomers of adenosylcobalamin Lactobacillus leichmannii ?
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?

Synonyms

Synonyms Comment Organism
ribonucleoside triphosphate reductase
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Lactobacillus leichmannii
RTPR
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Lactobacillus leichmannii