1998
DOI: 10.1016/s0014-5793(98)01575-0
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Kinetic properties and stereospecificity of the monomeric dUTPase from herpes simplex virus type 1

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 k cat /K M of about 10 7 M 31 s 31 and a K M of 0.3 W WM. However, the viral enzymes are less specific than the bacterial enzyme. The HSV and E. coli dUTPases show the same stereospecificit… Show more

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Cited by 20 publications
(19 citation statements)
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“…1A), with motif V invisible due to its flexibility, and revealed an active site that is extremely similar to those of trimeric dUTPases. EBV dUTPase furthermore exhibited similar kinetic parameters (17,18). This therefore implies that the conclusions of studies of the enzymatic mechanism for trimeric dUTPases are also valid for the EBV enzyme and vice versa.…”
supporting
confidence: 57%
“…1A), with motif V invisible due to its flexibility, and revealed an active site that is extremely similar to those of trimeric dUTPases. EBV dUTPase furthermore exhibited similar kinetic parameters (17,18). This therefore implies that the conclusions of studies of the enzymatic mechanism for trimeric dUTPases are also valid for the EBV enzyme and vice versa.…”
supporting
confidence: 57%
“…If this were the case, overexpression of other functional dUTPases would also be expected to cause downregulation of NKp44L. Therefore, we transiently transfected 293 cells with plasmids encoding Flagtagged ORF54 homologs from two other human herpesviruses, EBV (BLLF3), and HSV-1 (UL50), both of which have been shown to possess dUTPase activity (5,7,44). Cells were harvested after 48 h, and surface expression of NKp44L was compared to that of cells transfected with empty vector.…”
Section: Resultsmentioning
confidence: 99%
“…About 20 mg of soluble recombinant protein was obtained per liter of E. coli culture. dUTPases from various sources function as either monomers (3,4), dimers (20), or trimers (6,8,26,28,32). Recently, a bifunctional enzyme with dUTPase activity from Methanococcus jannaschii was discovered that functions as a hexamer (21).…”
Section: Resultsmentioning
confidence: 99%