The dUTPases from herpes simplex virus type 1 and mouse mammary tumour virus are less specific than the Escherichia coli enzyme
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/126258
- author
- Björnberg, Olof LU and Nyman, Per-Olof LU
- organization
- publishing date
- 1996
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of General Virology
- volume
- 77
- issue
- 12
- pages
- 3107 - 3111
- publisher
- Microbiology Society
- external identifiers
-
- scopus:0030462573
- ISSN
- 1465-2099
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Biochemistry and Structural Biology (S) (000006142), Biology building (Closed 2011) (011008000)
- id
- 32224f8e-d49a-4ce6-9f40-4786034b20c5 (old id 126258)
- alternative location
- http://vir.sgmjournals.org/cgi/reprint/77/12/3107
- date added to LUP
- 2016-04-01 15:52:38
- date last changed
- 2022-02-12 18:16:27
@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 = {{Microbiology Society}}, 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}}, url = {{http://vir.sgmjournals.org/cgi/reprint/77/12/3107}}, volume = {{77}}, year = {{1996}}, }