dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition

Johan Nord, Gunilla Larsson, Jan-Olov Kvassman, Anna Maria Rosengren, Per-Olof Nyman

Research output: Contribution to journalArticlepeer-review

Abstract

The kinetic properties of dUTPase from equine infectious anemia virus (EIAV) were investigated. KM (1.1 [plusmn] 0.1 [mu ]M) and kcat (25 s[minus ]1) were found to be independent of pH in the neutral pH range. Above pH 8.0, KM increases slightly. Below pH 6.0, the enzyme is rapidly deactivated. Detergent was found to enhance activity, leaving KM and kcat unaffected. Compared to the Escherichia coli dUTPase, the EIAV enzyme is equally potent in hydrolyzing dUTP, but less specific. Inhibition of the viral enzyme by the nucleotides dTTP, dUMP and a synthetic analogue, 2[prime ]-deoxyuridine 5[prime ]-([alpha ],[beta ]-imido)triphosphate, is stronger by one order of magnitude.
Original languageEnglish
Pages (from-to)271-274
JournalFEBS Letters
Volume414
Issue number2
DOIs
Publication statusPublished - 1997

Subject classification (UKÄ)

  • Biological Sciences

Free keywords

  • dUTPase
  • Equine infectious anemia virus
  • Kinetic constant
  • Inhibition
  • Deoxyuridine
  • Analogue

Fingerprint

Dive into the research topics of 'dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition'. Together they form a unique fingerprint.

Cite this