title: Antiviral nucleoside analogs phosphorylation by nucleoside diphosphate kinase.
abstract: The reaction of NDP kinase was studied in vitro with several antiviral derivatives, using kinetic steady state and presteady state analysis. The enzyme is highly efficient with natural nucleotides but most of the analogs are slow substrates. The catalytic efficiency, also related to the affinity of the analog, is mainly dependent on the presence of a 3'-OH group on the ribose moiety.
authors.affiliation: Institut Pasteur, Unité de Régulation Enzymatique des Activités Cellulaires, CNRS URA 2185, 25, rue du Dr. Roux, 75724 Paris Cedex 15, France.
authors.forename: S
authors.initials: S
authors.lastname: Gallois-Montbrun
authors.forename: M
authors.initials: M
authors.lastname: Veron
authors.forename: D
authors.initials: D
authors.lastname: Deville-Bonne
mesh_terms: D000998:Antiviral Agents / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D009701:Nucleoside-Diphosphate Kinase / Q000378:metabolism*; D009705:Nucleosides / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D000998:Antiviral Agents; D009705:Nucleosides; D009701:Nucleoside-Diphosphate Kinase