Related Experiment Video
Updated: Aug 12, 2026

Nucleoside Triphosphates - From Synthesis to Biochemical Characterization
Published on: April 3, 2014
Antiviral nucleoside analogs phosphorylation by nucleoside diphosphate kinase
S Gallois-Montbrun1, M Veron, D Deville-Bonne
1Institut Pasteur, Unité de Régulation Enzymatique des Activités Cellulaires, CNRS URA 2185, 25, rue du Dr. Roux, 75724 Paris Cedex 15, France.
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.
More Related Videos
08:17A High-Throughput Enzyme-Coupled Activity Assay to Probe Small Molecule Interaction with the dNTPase SAMHD1
Published on: April 16, 2021
10:29Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors
Published on: May 9, 2025
Related Concept Videos
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
DNA Base Pairing
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Biosynthesis of Nucleic Acids
Inhibitors of Viral Protein Synthesis
Antiviral Nucleoside Inhibitors