Enzyme-Substrate Interactions in the Purine-specific Nucleoside Hydrolase from Trypanosoma vivax

We previously reported the first x-ray structure of an inosine-adenosineguanosine preferring nucleoside hydrolase ) from Trypanosoma vivax

Wim Versées


Scholarcy highlights

  • The atomic coordinates and structure factors have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ
  • On the basis of their substrate specificity the nucleoside hydrolases have been divided into three subclasses: the base aspecific inosine-uridine preferring nucleoside hydrolases), the purine-specific inosine-adenosineguanosine preferring nucleoside hydrolases, and the 6-oxo-purine specific inosine-guanosine preferring nucleoside hydrolases
  • In this paper we reported the crystal structures of the D10A mutant of the IAG-NH from T. vivax in complex with the inhibitor 3-deaza-adenosine and the substrate inosine
  • The danger of overinterpreting enzyme-inhibitor complexes is pointed out, as the natural substrate inosine is bound in a different conformation to the active site as the substrate analogue inhibitor, 3-deaza-adenosine
  • We examined the substrate specificity of the IAG-NH
  • The presence of a general acid involved in protonating the leaving group was inferred from the pH profile and previous studies with the IU-NH from C. fasciculata
  • An alternative mechanism to activate the leaving group, by increasing its pKa, through the parallel aromatic stacking interaction is proposed

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