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

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

Sammanfattning

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.
Originalspråkengelska
Sidor (från-till)271-274
TidskriftFEBS Letters
Volym414
Nummer2
DOI
StatusPublished - 1997

Ämnesklassifikation (UKÄ)

  • Biologiska vetenskaper

Fingeravtryck

Utforska forskningsämnen för ”dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition”. Tillsammans bildar de ett unikt fingeravtryck.

Citera det här