Ribonucleotide reductase of herpes simplex virus type 2 resembles that of herpes simplex virus type 1.

Abstract

The ribonucleotide reductase (ribonucleoside-diphosphate reductase; EC 1.17.4.1) induced by herpes simplex virus type 2 infection of serum-starved BHK-21 cells was purified to provide a preparation practically free of both eucaryotic ribonucleotide reductase and contaminating enzymes that could significantly deplete the substrates. Certain key properties of the herpes simplex virus type 2 ribonucleotide reductase were examined to define the extent to which it resembled the herpes simplex virus type 1 ribonucleotide reductase. The herpes simplex virus type 2 ribonucleotide reductase was inhibited by ATP and MgCl2 but only weakly inhibited by the ATP X Mg complex. Deoxynucleoside triphosphates were at best only weak inhibitors of this enzyme. ADP was a competitive inhibitor (K'i, 11 microM) of CDP reduction (K'm, 0.5 microM), and CDP was a competitive inhibitor (K'i, 0.4 microM) of ADP reduction (K'm, 8 microM). These key properties closely resemble those observed for similarly purified herpes simplex virus type 1 ribonucleotide reductase and serve to distinguish these virally induced enzymes from other ribonucleotide reductases.

• Authors: D R Averett, P A Furman, T Spector
• Journal: Journal of virology (J Virol) Vol. 52 Issue 3 Pg. 981-3 (Dec 1984) ISSN: 0022-538X [Print] United States
• PMID: 6092726 (Publication Type: Journal Article)

Chemical References

• Cytidine Diphosphate
• Adenosine Triphosphate
• Ribonucleotide Reductases
• Magnesium

Topics

• Adenosine Triphosphate (pharmacology)
• Cytidine Diphosphate (metabolism)
• Kinetics
• Magnesium (pharmacology)
• Ribonucleotide Reductases (antagonists & inhibitors, isolation & purification)
• Simplexvirus (enzymology)