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dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition

Nord, Johan; Larsson, Gunilla; Kvassman, Jan-Olov; Rosengren, Anna Maria and Nyman, Per-Olof LU (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.
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author
organization
publishing date
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
2007-07-09 08:38:16
date last changed
2017-01-01 06:59:18
@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},
  keyword      = {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},
  volume       = {414},
  year         = {1997},
}