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dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition
Author(s) -
Johan Nord,
Gunilla Larsson,
Jan Kvassman,
Anna Rosengren,
Per Olof Nyman
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00935-6
Subject(s) - equine infectious anemia , enzyme , escherichia coli , chemistry , nucleotide , retrovirus , virus , virology , microbiology and biotechnology , deoxyuridine , biochemistry , enzyme assay , biology , dna , gene
The kinetic properties of dUTPase from equine infectious anemia virus (EIAV) were investigated. K M (1.1 ± 0.1 μM) 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 deactivated. Detergent was found to enhance activity, leaving K M and k cat 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′‐deoxyuridine 5′‐(α,β‐imido)triphosphate, is stronger by one order of magnitude.