DUTPASE FROM THE RETROVIRUS EQUINE INFECTIOUS-ANEMIA VIRUS - SPECIFICITY, TURNOVER AND INHIBITION

The kinetic properties of dUTPase from equine infectious anemia virus (EIAV) were investigated, K-M (1.1 +/- 0.1 mu M) and k(cat) (25 s(-1)) were found to be independent of pH in the neutral pH range, Above pH 8.0, K-M increases slightly, Below pH 6.0, the enzyme is rapidly deact ivated, Detergent was found to enhance activity, leaving K-M and k(cat ) unaffected, Compared to the Escherichia coli dUTPase, the EIAV enzym e is equally potent in hydrolyzing dUTP, but less specific, Inhibition of the viral enzyme by the nucleotides dTTP, dUMP and a synthetic ana logue, 2'-deoxyuridine 5'-(alpha,beta-imido)triphosphate, is stronger by one order of magnitude. (C) 1997 Federation of European Biochemical Societies.