dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition
(1997) In FEBS Letters 414(2). p.271-274- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/126198
- author
- Nord, Johan ; Larsson, Gunilla ; Kvassman, Jan-Olov ; Rosengren, Anna Maria and Nyman, Per-Olof LU
- organization
- publishing date
- 1997
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- dUTPase, Equine infectious anemia virus, Kinetic constant, Inhibition, Deoxyuridine, Analogue
- in
- FEBS Letters
- volume
- 414
- issue
- 2
- pages
- 271 - 274
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:0031559946
- ISSN
- 1873-3468
- DOI
- 10.1016/S0014-5793(97)00935-6
- language
- English
- LU publication?
- yes
- id
- b4a8cf21-1a74-4544-a504-c41f16fc60ee (old id 126198)
- date added to LUP
- 2016-04-01 16:13:32
- date last changed
- 2022-01-28 18:12:13
@article{b4a8cf21-1a74-4544-a504-c41f16fc60ee, 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.}}, author = {{Nord, Johan and Larsson, Gunilla and Kvassman, Jan-Olov and Rosengren, Anna Maria and Nyman, Per-Olof}}, issn = {{1873-3468}}, keywords = {{dUTPase; Equine infectious anemia virus; Kinetic constant; Inhibition; Deoxyuridine; Analogue}}, language = {{eng}}, number = {{2}}, pages = {{271--274}}, publisher = {{Wiley-Blackwell}}, series = {{FEBS Letters}}, title = {{dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition}}, url = {{http://dx.doi.org/10.1016/S0014-5793(97)00935-6}}, doi = {{10.1016/S0014-5793(97)00935-6}}, volume = {{414}}, year = {{1997}}, }