Abstract:
:The kinetic properties of dUTPase from equine infectious anemia virus (EIAV) were investigated. K(M) (1.1 +/- 0.1 microM) 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'-(alpha,beta-imido)triphosphate, is stronger by one order of magnitude.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Nord J,Larsson G,Kvassman JO,Rosengren AM,Nyman POdoi
10.1016/s0014-5793(97)00935-6subject
Has Abstractpub_date
1997-09-08 00:00:00pages
271-4issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00935-6journal_volume
414pub_type
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