Phosphorylation of anti-HIV nucleoside analogs by nucleoside diphosphate kinase.
The reaction of NDP kinase with antiviral nucleoside triphosphates used in antiviral therapies was studied at the presteady state by fluorescence stopped-flow and compared with the steady-state parameters. The affinity of the analogs was determined by fluorescence titration of a mutated enzyme with an inserted Trp in the binding site. The lack of the 3' hydroxyl in analogs is shown to decrease the kcat more than the KD.
Schneider
B
B
Unité de Régulation Enzymatique des Activités Cellulaires, CNRS URA1773, Institut Pasteur, Paris, France.
Xu
Y
Y
Sellam
O
O
Sarfati
R
R
Janin
J
J
Véron
M
M
Deville-Bonne
D
D
D019380:Anti-HIV Agents / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000378:metabolism / Q000494:pharmacology; D007700:Kinetics; D009701:Nucleoside-Diphosphate Kinase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009705:Nucleosides / Q000378:metabolism*; D010766:Phosphorylation; D013379:Substrate Specificity
D019380:Anti-HIV Agents; D004791:Enzyme Inhibitors; D009705:Nucleosides; D009701:Nucleoside-Diphosphate Kinase