Kinetic properties and stereospecificity of the monomeric dUTPase from herpes simplex virus type 1

Research output: Contribution to journalArticle

Abstract

Kinetic properties of the monomeric enzyme dUTPase from herpes simplex virus type 1 (HSV) were investigated and compared to those previously determined for homotrimeric dUTPases of bacterial and retroviral origins. The HSV and Escherichia coli dUTPases are equally potent as catalysts towards the native substrate dUTP with a kcat/KM of about 107 M-1 s-1 and a KM of 0.3 μM. However, the viral enzymes are less specific than the bacterial enzyme. The HSV and E. coli dUTPases show the same stereospecificity towards the racemic substrate analogue dUTPαS (2'-deoxyuridine 5'-(α-thio)triphosphate), suggesting that they have identical reaction mechanisms.

Details

Authors
  • Anna-Carin Bergman
  • Per-Olof Nyman
  • Gunilla Larsson
Organisations
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences

Keywords

  • dUTPase, Nucleotide metabolism, Kinetics, Inhibition, Substrate analogue, Herpes simplex virus
Original languageEnglish
Pages (from-to)327-330
JournalFEBS Letters
Volume441
Issue number2
Publication statusPublished - 1998
Publication categoryResearch
Peer-reviewedYes