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Literature summary for 2.7.7.49 extracted from

  • Deval, J.; Alvarez, K.; Selmi, B.; Bermond, M.; Boretto, J.; Guerreiro, C.; Mulard, L.; Canard, B.
    Mechanistic insights into the suppression of drug resistance by human immunodeficiency virus type 1 reverse transcriptase using alpha-boranophosphate nucleoside analogs (2005), J. Biol. Chem., 280, 3838-3846.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
borano-3TCTP alpha-Boranophosphate nucleoside analogs enhance 3–8fold the binding of Mg2+ ions to the active site of the enzyme-DNA-dNTP complex and alleviate the requirement of critical amino acids involved in phosphodiester bond formation Human immunodeficiency virus 1
borano-dTTP 100fold decrease in polymerase activity caused by the R72A substitution is restored to wild-type levels using borano-dTTP. alpha-Boranophosphate nucleoside analogs enhance 3–8fold the binding of Mg2+ ions to the active site of the enzyme-DNA-dNTP complex and alleviate the requirement of critical amino acids involved in phosphodiester bond formation Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
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