Antiviral Nucleoside Analogs Phosphorylation by Nucleoside Diphosphate Kinase

S.      Gallois-Montbrun; M.      Veron; D.      Deville-Bonne

doi:10.2174/1389557043403990

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.

Keywords: ndp kinase, antiviral nucleoside analog, dideoxynucleoside, acyclovir, azt, d4t, 3tc, borano substitution

« Previous Next »

Rights & Permissions Print Cite

Mini-Reviews in Medicinal Chemistry

Title: Antiviral Nucleoside Analogs Phosphorylation by Nucleoside Diphosphate Kinase

Volume: 4 Issue: 4

Author(s): S. Gallois-Montbrun, M. Veron and D. Deville-Bonne

Affiliation:

Keywords: ndp kinase, antiviral nucleoside analog, dideoxynucleoside, acyclovir, azt, d4t, 3tc, borano substitution

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.

Export Options

Export File:

RIS (for EndNote, Reference Manager, ProCite)

BibTeX

Text

Content:

Citation Only

Citation and Abstract

About this article

Cite this article as:

Gallois-Montbrun S., Veron M. and Deville-Bonne D., Antiviral Nucleoside Analogs Phosphorylation by Nucleoside Diphosphate Kinase, Mini-Reviews in Medicinal Chemistry 2004; 4 (4) . https://dx.doi.org/10.2174/1389557043403990