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The dUTPases from herpes simplex virus type 1 and mouse mammary tumour virus are less specific than the Escherichia coli enzyme

Björnberg, Olof LU and Nyman, Per-Olof LU (1996) In Journal of General Virology 77(12). p.3107-3111
Abstract
The enzyme dUTPase catalyses the hydrolysis of dUTP to dUMP and pyrophosphate, thereby suppressing incorporation of uracil into DNA and providing a pool of dUMP, the precursor of dTTP. Hydrolysis of other nucleotides similar in structure to dUTP would conceivably be physiologically detrimental and high specificity of the reaction seems to be necessary. In this work, we characterize the substrate specificity of the dUTPases from herpes simplex virus type 1 (HSV-1) and mouse mammary tumour virus (MMTV) in comparison to the Escherichia coli enzyme. We tested dCTP, dTTP, UTP and dUDP as substrates. Significantly higher reactivity was observed for the HSV-1 enzyme with dCTP and dTTP and for the MMTV enzyme with dTTP and UTP. The lower substrate... (More)
The enzyme dUTPase catalyses the hydrolysis of dUTP to dUMP and pyrophosphate, thereby suppressing incorporation of uracil into DNA and providing a pool of dUMP, the precursor of dTTP. Hydrolysis of other nucleotides similar in structure to dUTP would conceivably be physiologically detrimental and high specificity of the reaction seems to be necessary. In this work, we characterize the substrate specificity of the dUTPases from herpes simplex virus type 1 (HSV-1) and mouse mammary tumour virus (MMTV) in comparison to the Escherichia coli enzyme. We tested dCTP, dTTP, UTP and dUDP as substrates. Significantly higher reactivity was observed for the HSV-1 enzyme with dCTP and dTTP and for the MMTV enzyme with dTTP and UTP. The lower substrate specificity of the two virus enzymes compared with the bacterial enzyme is discussed in relation to the DNA precursor metabolism during virus replication. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of General Virology
volume
77
issue
12
pages
3107 - 3111
publisher
Society for General Microbiology
external identifiers
  • scopus:0030462573
ISSN
1465-2099
language
English
LU publication?
yes
id
32224f8e-d49a-4ce6-9f40-4786034b20c5 (old id 126258)
alternative location
http://vir.sgmjournals.org/cgi/reprint/77/12/3107
date added to LUP
2007-07-04 13:48:55
date last changed
2017-01-01 06:49:16
@article{32224f8e-d49a-4ce6-9f40-4786034b20c5,
  abstract     = {The enzyme dUTPase catalyses the hydrolysis of dUTP to dUMP and pyrophosphate, thereby suppressing incorporation of uracil into DNA and providing a pool of dUMP, the precursor of dTTP. Hydrolysis of other nucleotides similar in structure to dUTP would conceivably be physiologically detrimental and high specificity of the reaction seems to be necessary. In this work, we characterize the substrate specificity of the dUTPases from herpes simplex virus type 1 (HSV-1) and mouse mammary tumour virus (MMTV) in comparison to the Escherichia coli enzyme. We tested dCTP, dTTP, UTP and dUDP as substrates. Significantly higher reactivity was observed for the HSV-1 enzyme with dCTP and dTTP and for the MMTV enzyme with dTTP and UTP. The lower substrate specificity of the two virus enzymes compared with the bacterial enzyme is discussed in relation to the DNA precursor metabolism during virus replication.},
  author       = {Björnberg, Olof and Nyman, Per-Olof},
  issn         = {1465-2099},
  language     = {eng},
  number       = {12},
  pages        = {3107--3111},
  publisher    = {Society for General Microbiology},
  series       = {Journal of General Virology},
  title        = {The dUTPases from herpes simplex virus type 1 and mouse mammary tumour virus are less specific than the Escherichia coli enzyme},
  volume       = {77},
  year         = {1996},
}