Phosphorylation of nucleosides and nucleoside analogs by mammalian nucleoside monophosphate kinases

Pharmacol Ther. Aug-Sep 2000;87(2-3):189-98. doi: 10.1016/s0163-7258(00)00048-6.

Abstract

Nucleoside monophosphate kinases catalyze the reversible phosphotransferase reaction between nucleoside triphosphates and monophosphates, i.e., monophosphates are converted to their corresponding diphosphate form. These enzymes play an important role in the synthesis of nucleotides that are required for a variety of cellular metabolic processes, as well as for RNA and DNA synthesis. Human tissues contain a thymidylate kinase, a uridylate-cytidylate kinase, five isozymes of adenylate kinase, and several guanylate kinases. Nucleoside monophosphate kinases are also required for the pharmacological activation of therapeutic nucleoside and nucleotide analogs. This overview is focused on the substrate specificity, tissue distribution, and subcellular location of the mammalian monophosphate kinases and their role in the activation of nucleoside and nucleotide analogs.

Publication types

  • Review

MeSH terms

  • Animals
  • Cell Cycle / physiology
  • Humans
  • Mammals / physiology
  • Nucleoside-Phosphate Kinase / metabolism*
  • Nucleoside-Phosphate Kinase / pharmacokinetics
  • Nucleosides / metabolism*
  • Nucleotides / metabolism*
  • Phosphorylation
  • Phosphotransferases / metabolism
  • Substrate Specificity
  • Tissue Distribution

Substances

  • Nucleosides
  • Nucleotides
  • Phosphotransferases
  • Nucleoside-Phosphate Kinase