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Kinetic properties and stereospecificity of the monomeric dUTPase from herpes simplex virus type 1

Bergman, Anna-Carin; Nyman, Per-Olof LU and Larsson, Gunilla (1998) In FEBS Letters 441(2). p.327-330
Abstract
Kinetic properties of the monomeric enzyme dUTPase from herpes simplex virus type 1 (HSV) were investigated and compared to those previously determined for homotrimeric dUTPases of bacterial and retroviral origins. The HSV and Escherichia coli dUTPases are equally potent as catalysts towards the native substrate dUTP with a kcat/KM of about 107 M-1 s-1 and a KM of 0.3 μM. However, the viral enzymes are less specific than the bacterial enzyme. The HSV and E. coli dUTPases show the same stereospecificity towards the racemic substrate analogue dUTPαS (2'-deoxyuridine 5'-(α-thio)triphosphate), suggesting that they have identical reaction mechanisms.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
dUTPase, Nucleotide metabolism, Kinetics, Inhibition, Substrate analogue, Herpes simplex virus
in
FEBS Letters
volume
441
issue
2
pages
327 - 330
publisher
Wiley-Blackwell
external identifiers
  • scopus:0032433501
ISSN
1873-3468
DOI
10.1016/S0014-5793(98)01575-0
language
English
LU publication?
yes
id
ce3467d4-4451-4302-8908-a5af9443aa31 (old id 125478)
date added to LUP
2007-07-04 12:07:14
date last changed
2017-01-01 07:15:22
@article{ce3467d4-4451-4302-8908-a5af9443aa31,
  abstract     = {Kinetic properties of the monomeric enzyme dUTPase from herpes simplex virus type 1 (HSV) were investigated and compared to those previously determined for homotrimeric dUTPases of bacterial and retroviral origins. The HSV and Escherichia coli dUTPases are equally potent as catalysts towards the native substrate dUTP with a kcat/KM of about 107 M-1 s-1 and a KM of 0.3 μM. However, the viral enzymes are less specific than the bacterial enzyme. The HSV and E. coli dUTPases show the same stereospecificity towards the racemic substrate analogue dUTPαS (2'-deoxyuridine 5'-(α-thio)triphosphate), suggesting that they have identical reaction mechanisms.},
  author       = {Bergman, Anna-Carin and Nyman, Per-Olof and Larsson, Gunilla},
  issn         = {1873-3468},
  keyword      = {dUTPase,Nucleotide metabolism,Kinetics,Inhibition,Substrate analogue,Herpes simplex virus},
  language     = {eng},
  number       = {2},
  pages        = {327--330},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {Kinetic properties and stereospecificity of the monomeric dUTPase from herpes simplex virus type 1},
  url          = {http://dx.doi.org/10.1016/S0014-5793(98)01575-0},
  volume       = {441},
  year         = {1998},
}